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    UBE2V2 ubiquitin conjugating enzyme E2 V2 [ Homo sapiens (human) ]

    Gene ID: 7336, updated on 10-Dec-2024

    GeneRIFs: Gene References Into Functions

    GeneRIFPubMed TitleDate
    UBE2V2 promotes metastasis by regulating EMT and predicts a poor prognosis in lung adenocarcinoma.

    UBE2V2 promotes metastasis by regulating EMT and predicts a poor prognosis in lung adenocarcinoma.
    Yang Z, Wu G, Zhao J, Shi G, Zhou J, Zhou X., Free PMC Article

    11/1/2023
    UBE2V2 Positively Correlates With PD-L1 Expression and Confers Poor Patient Survival in Lung Adenocarcinoma.

    UBE2V2 Positively Correlates With PD-L1 Expression and Confers Poor Patient Survival in Lung Adenocarcinoma.
    Hua ZD, Liu XB, Sheng JH, Li C, Li P, Cai XQ, Han ZQ.

    02/5/2022
    Uev1A amino terminus stimulates poly-ubiquitin chain assembly and is required for NF-kappaB activation.

    Uev1A amino terminus stimulates poly-ubiquitin chain assembly and is required for NF-κB activation.
    Wu Z, Andersen PL, Moraes T, McKenna SA, Zhang Y, Zhang W, Ellison MJ, Xiao W.

    10/23/2021
    Ubc13-Mms2 cooperates with a family of RING E3 proteins in budding yeast membrane protein sorting.

    Ubc13-Mms2 cooperates with a family of RING E3 proteins in budding yeast membrane protein sorting.
    Renz C, Albanèse V, Tröster V, Albert TK, Santt O, Jacobs SC, Khmelinskii A, Léon S, Ulrich HD.

    07/31/2021
    Data suggest that ubiquitin-conjugating enzyme E2 variant 2 (Ube2V2) and ring finger protein 4 (RNF4) together induce an active conformation of the ubiquitin-conjugating enzyme Ubc13-ubiquitin (Ubc13~Ub) thioester.

    Structural basis for the RING-catalyzed synthesis of K63-linked ubiquitin chains.
    Branigan E, Plechanovová A, Jaffray EG, Naismith JH, Hay RT., Free PMC Article

    11/28/2015
    Functional analysis of selected regulated proteins revealed that knockdown of HNRPD, PHB2 and UB2V2 can increase HCMV replication, while knockdown of A4 and KSRP resulted in decreased HCMV replication.

    Subcellular quantitative proteomic analysis reveals host proteins involved in human cytomegalovirus infection.
    Chai F, Li HY, Wang W, Zhu XJ, Li Y, Wang S, Guo L, Zhang LK, Xiao G.

    08/22/2015
    suppression of hMMS2 reverses L-OHP tolerance in differentiated human colorectal carcinoma cells by promoting apoptosis

    [Roles of hMMS2 gene in reversing the oxaliplatin tolerance of human colon carcinoma cells].
    Zhang L, Sui Y, Wang T, Li L, Li Y, Jin C, Xu F.

    06/14/2014
    Data show RING finger (RNF) E3 ubiquitin ligase RNF8 dimerizes and binds to E2 ubiquitin-conjugating complex Ubc13/Mms2 with formation of Lys-63 ubiquitin chains, whereas the RNF168 RING domain is a monomer and does not catalyze Lys-6 ubiquitylation.

    Molecular insights into the function of RING finger (RNF)-containing proteins hRNF8 and hRNF168 in Ubc13/Mms2-dependent ubiquitylation.
    Campbell SJ, Edwards RA, Leung CC, Neculai D, Hodge CD, Dhe-Paganon S, Glover JN., Free PMC Article

    10/13/2012
    the crystal structure of human OTUB1 in complex with human UBC13 and MMS2

    Molecular basis of Lys-63-linked polyubiquitination inhibition by the interaction between human deubiquitinating enzyme OTUB1 and ubiquitin-conjugating enzyme UBC13.
    Sato Y, Yamagata A, Goto-Ito S, Kubota K, Miyamoto R, Nakada S, Fukai S., Free PMC Article

    10/13/2012
    entire coding region and splice junctions of RNF8, UBC13 and MMS2 genes were screened for mutations in affected index cases from 123 Northern Finnish breast cancer families

    Mutation screening of the RNF8, UBC13 and MMS2 genes in Northern Finnish breast cancer families.
    Vuorela M, Pylkäs K, Winqvist R., Free PMC Article

    10/8/2011
    These results point to a high level of redundancy in the DNA damage tolerance pathway and suggest the existence of another hMMS2 variant (hMMSv) or complex that can compensate for its loss.

    hMMS2 serves a redundant role in human PCNA polyubiquitination.
    Brun J, Chiu R, Lockhart K, Xiao W, Wouters BG, Gray DA., Free PMC Article

    01/21/2010
    Mms2 physical association with ubiquitin is correlated with its ability to promote Lys63-linked ubiquitin chain assembly

    Two Mms2 residues cooperatively interact with ubiquitin and are critical for Lys63 polyubiquitination in vitro and in vivo.
    Pastushok L, Spyracopoulos L, Xiao W.

    01/21/2010
    Data demonstrate that divergent activities of Ubc13 rely on its pairing with either of two Uevs, Uev1A or Mms2.

    Distinct regulation of Ubc13 functions by the two ubiquitin-conjugating enzyme variants Mms2 and Uev1A.
    Andersen PL, Zhou H, Pastushok L, Moraes T, McKenna S, Ziola B, Ellison MJ, Dixit VM, Xiao W., Free PMC Article

    01/21/2010
    The results in this study allowed identification of important residues of the Ubc13-Mms2 interface, determine a correlation between heterodimer formation and function, and conclude why Mms2 forms a specific complex with Ubc13 but not other Ubc proteins.

    A single Mms2 "key" residue insertion into a Ubc13 pocket determines the interface specificity of a human Lys63 ubiquitin conjugation complex.
    Pastushok L, Moraes TF, Ellison MJ, Xiao W.

    01/21/2010
    Ubc13-Mms2 and Lys63-polyubiquitin chains are associated with signaling cellular stress

    The Chfr mitotic checkpoint protein functions with Ubc13-Mms2 to form Lys63-linked polyubiquitin chains.
    Bothos J, Summers MK, Venere M, Scolnick DM, Halazonetis TD.

    01/21/2010
    UBE2v2 signalling through PCNA ubiquitination is not required for immunoglobulin diversification in DT40 cells.

    UBE2V2 (MMS2) is not required for effective immunoglobulin gene conversion or DNA damage tolerance in DT40.
    Simpson LJ, Sale JE.

    01/21/2010
    Insight into the influence of protein dynamics on the affinity of ubiquitin for Mms2.

    Main chain and side chain dynamics of the ubiquitin conjugating enzyme variant human Mms2 in the free and ubiquitin-bound States.
    Spyracopoulos L, Lewis MJ, Saltibus LF.

    01/21/2010
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