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    UBE2D2 ubiquitin conjugating enzyme E2 D2 [ Homo sapiens (human) ]

    Gene ID: 7322, updated on 10-Oct-2024

    GeneRIFs: Gene References Into Functions

    GeneRIFPubMed TitleDate
    CircUBE2D2 regulates HMGB1 through miR-885-5p to promote ovarian cancer malignancy.

    CircUBE2D2 regulates HMGB1 through miR-885-5p to promote ovarian cancer malignancy.
    Yan R, Zeng S, Gao F, Li L, Xiao X., Free PMC Article

    06/20/2024
    The E2 ubiquitin-conjugating enzymes UBE2D1 and UBE2D2 regulate VEGFR2 dynamics and endothelial function.

    The E2 ubiquitin-conjugating enzymes UBE2D1 and UBE2D2 regulate VEGFR2 dynamics and endothelial function.
    Critchley WR, Smith GA, Zachary IC, Harrison MA, Ponnambalam S., Free PMC Article

    05/26/2023
    Exosomes Mediated Transfer of Circ_UBE2D2 Enhances the Resistance of Breast Cancer to Tamoxifen by Binding to MiR-200a-3p.

    Exosomes Mediated Transfer of Circ_UBE2D2 Enhances the Resistance of Breast Cancer to Tamoxifen by Binding to MiR-200a-3p.
    Hu K, Liu X, Li Y, Li Q, Xu Y, Zeng W, Zhong G, Yu C., Free PMC Article

    05/22/2021
    Ube2D2 was validated as a functional E2 enzyme for the ubiquitylation of the p53 transactivation domain (p53-TAD) by MUL1-RING, and purification and crystallization processes for MUL1-RING and the MUL1-RING-Ube2D2 complex are reported.

    The RING domain of mitochondrial E3 ubiquitin ligase 1 and its complex with Ube2D2: crystallization and X-ray diffraction.
    Lee SO, Lee CK, Ryu KS, Chi SW., Free PMC Article

    06/13/2020
    results disclose the mechanism by which cIAP1 RING dimer activates UbcH5B approximately Ub and indicate that noncovalent Ubiquitin (Ub) binding further stabilizes the cIAP1-UbcH5B approximately Ubiquitin (Ub) complex in the active conformation to stimulate Ub transfer

    Structural insights into non-covalent ubiquitin activation of the cIAP1-UbcH5B∼ubiquitin complex.
    Patel A, Sibbet GJ, Huang DT., Free PMC Article

    05/4/2019
    These results point to an important role of the affinity between RNF4 and its cognate RAD6B or UBCH5B in governing the multiplicity of substrate ubiquitination.

    Role of E2-RING Interactions in Governing RNF4-Mediated Substrate Ubiquitination.
    DiBello A, Datta AB, Zhang X, Wolberger C., Free PMC Article

    07/1/2017
    Knockdown of UBE2D2 caused an increase in p53 protein levels, and knockdown of p53 attenuated not only cadmium-induced apoptosis, but also cadmium-induced apoptosis-related gene expression.

    Accumulation of p53 via down-regulation of UBE2D family genes is a critical pathway for cadmium-induced renal toxicity.
    Lee JY, Tokumoto M, Fujiwara Y, Hasegawa T, Seko Y, Shimada A, Satoh M., Free PMC Article

    12/24/2016
    mutations having marked effects on function only minimally affect the intermolecular interactions between the AO7 RING and UbcH5B, establishing a high degree of complexity in activation through the RING-E2 interface.

    Insights into Ubiquitination from the Unique Clamp-like Binding of the RING E3 AO7 to the E2 UbcH5B.
    Li S, Liang YH, Mariano J, Metzger MB, Stringer DK, Hristova VA, Li J, Randazzo PA, Tsai YC, Ji X, Weissman AM., Free PMC Article

    04/23/2016
    Data show that ubiquitin E2 enzymes UBE2D1/2/3 and E3 ligase RNF138 accumulate at DNA-damage sites and act at early resection stages by promoting CtIP protein ubiquitylation and accrual.

    Systematic E2 screening reveals a UBE2D-RNF138-CtIP axis promoting DNA repair.
    Schmidt CK, Galanty Y, Sczaniecka-Clift M, Coates J, Jhujh S, Demir M, Cornwell M, Beli P, Jackson SP., Free PMC Article

    03/19/2016
    together with UBE2L3 and UBE2N, synergistically contribute to Parkin-mediated mitophagy

    The ubiquitin-conjugating enzymes UBE2N, UBE2L3 and UBE2D2/3 are essential for Parkin-dependent mitophagy.
    Geisler S, Vollmer S, Golombek S, Kahle PJ.

    10/24/2015
    Presented is the structure of the human dimeric RING domain from BIRC7 in complex with the E2 UbcH5B covalently linked to Ub.

    BIRC7-E2 ubiquitin conjugate structure reveals the mechanism of ubiquitin transfer by a RING dimer.
    Dou H, Buetow L, Sibbet GJ, Cameron K, Huang DT., Free PMC Article

    11/17/2012
    Observational study of gene-disease association, gene-environment interaction, and pharmacogenomic / toxicogenomic. (HuGE Navigator)

    Variation at the NFATC2 locus increases the risk of thiazolidinedione-induced edema in the Diabetes REduction Assessment with ramipril and rosiglitazone Medication (DREAM) study.
    Bailey SD, Xie C, Do R, Montpetit A, Diaz R, Mohan V, Keavney B, Yusuf S, Gerstein HC, Engert JC, Anand S, DREAM investigators., Free PMC Article

    09/15/2010
    Whereas UbcH5(A, B and C) is highly efficient in converting IkBa into monoubiquitinated forms, Cdc34 drives ubiquitin (Ub)-Ub conjugation

    Priming and extending: a UbcH5/Cdc34 E2 handoff mechanism for polyubiquitination on a SCF substrate.
    Wu K, Kovacev J, Pan ZQ., Free PMC Article

    05/3/2010
    determined the 2.2 A crystal structure of an intermediate of UbcH5b approximately ubiquitin (Ub) conjugate, which is assembled into an infinite spiral through the backside interaction.

    Crystal structure of UbcH5b~ubiquitin intermediate: insight into the formation of the self-assembled E2~Ub conjugates.
    Sakata E, Satoh T, Yamamoto S, Yamaguchi Y, Yagi-Utsumi M, Kurimoto E, Tanaka K, Wakatsuki S, Kato K.

    05/3/2010
    role of WW3 and WW4 domains of Nedd4-2 in dopamine transporter ubiquitination was demonstrated; siRNA analysis demonstrated that this polyubiquitination is mediated by Nedd4-2 cooperation with UBE2D and UBE2L3 E2 ubiquitin-conjugating enzymes

    Lysine 63-linked polyubiquitination of the dopamine transporter requires WW3 and WW4 domains of Nedd4-2 and UBE2D ubiquitin-conjugating enzymes.
    Vina-Vilaseca A, Sorkin A., Free PMC Article

    05/3/2010
    Results describe the crystal structure of a complex between the HECT domain of NEDD4L and the E2 UbcH5B bearing a covalently linked Ub at its active site (UbcH5B approximately Ub).

    Insights into ubiquitin transfer cascades from a structure of a UbcH5B approximately ubiquitin-HECT(NEDD4L) complex.
    Kamadurai HB, Souphron J, Scott DC, Duda DM, Miller DJ, Stringer D, Piper RC, Schulman BA., Free PMC Article

    02/8/2010
    Observational study of gene-disease association. (HuGE Navigator)See all PubMed (2) articles

    Gene-centric association signals for lipids and apolipoproteins identified via the HumanCVD BeadChip.
    Talmud PJ, Drenos F, Shah S, Shah T, Palmen J, Verzilli C, Gaunt TR, Pallas J, Lovering R, Li K, Casas JP, Sofat R, Kumari M, Rodriguez S, Johnson T, Newhouse SJ, Dominiczak A, Samani NJ, Caulfield M, Sever P, Stanton A, Shields DC, Padmanabhan S, Melander O, Hastie C, Delles C, Ebrahim S, Marmot MG, Smith GD, Lawlor DA, Munroe PB, Day IN, Kivimaki M, Whittaker J, Humphries SE, Hingorani AD, ASCOT investigators, NORDIL investigators, BRIGHT Consortium.

    Integrated genomic analysis implicates haploinsufficiency of multiple chromosome 5q31.2 genes in de novo myelodysplastic syndromes pathogenesis.
    Graubert TA, Payton MA, Shao J, Walgren RA, Monahan RS, Frater JL, Walshauser MA, Martin MG, Kasai Y, Walter MJ.

    03/25/2009
    The results imply that the interaction specificity between c-Cbl, UbcH7 and UbcH5b is required but not sufficient for transfer of ubiquitin to potential targets.

    E2-c-Cbl recognition is necessary but not sufficient for ubiquitination activity.
    Huang A, de Jong RN, Wienk H, Winkler GS, Timmers HT, Boelens R.

    01/21/2010
    Ubc4/5 and c-Cbl continue to ubiquitinate EGF receptor after internalization to facilitate polyubiquitination and degradation

    Ubc4/5 and c-Cbl continue to ubiquitinate EGF receptor after internalization to facilitate polyubiquitination and degradation.
    Umebayashi K, Stenmark H, Yoshimori T., Free PMC Article

    01/21/2010
    UBE2D2 is required for GCMa ubiquitination and for association with the SCF(FBXW2) complex.

    Ubiquitin-conjugating enzyme UBE2D2 is responsible for FBXW2 (F-box and WD repeat domain containing 2)-mediated human GCM1 (glial cell missing homolog 1) ubiquitination and degradation.
    Chiang MH, Chen LF, Chen H.

    01/21/2010
    Data show that binding of the CNOT4 RING finger to the ubiquitin-conjugating enzyme (E2) UbcH5B is highly selective.

    An altered-specificity ubiquitin-conjugating enzyme/ubiquitin-protein ligase pair.
    Winkler GS, Albert TK, Dominguez C, Legtenberg YI, Boelens R, Timmers HT.

    01/21/2010
    UbcH5B/C are E2s for Mdm2, which contribute to the maintenance of low levels of p53 and Mdm2 in unstressed cells; inhibition of p53 ubiquitination and degradation by targeting UbcH5B/C is not sufficient to up-regulate p53 transcriptional activity.

    Regulation of p53 by the ubiquitin-conjugating enzymes UbcH5B/C in vivo.
    Saville MK, Sparks A, Xirodimas DP, Wardrop J, Stevenson LF, Bourdon JC, Woods YL, Lane DP.

    01/21/2010
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