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Ubiquitin-conjugating enzyme E2M

Ubc12, hUbc12, NEDD8-conjugating enzyme UBC12
The modification of proteins 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. This gene encodes a member of the E2 ubiquitin-conjugating enzyme family. The encoded protein is linked with a ubiquitin-like protein, NEDD8, which can be conjugated to cellular proteins, such as Cdc53/culin. [provided by RefSeq, Jul 2008] (from NCBI)
Top mentioned proteins: NEDD8, Ubiquitin, Cullin, SCF, V1a
Papers on Ubc12
Flavokawain A induces deNEDDylation and Skp2 degradation leading to inhibition of tumorigenesis and cancer progression in the TRAMP transgenic mouse model.
Zi et al., Orange, United States. In Oncotarget, Jan 2016
Further studies have demonstrated that FKA docked into the ATP binding pocket of the precursor cell-expressed developmentally down-regulated 8 (NEDD8)-activating enzyme (NAE) complex, inhibited NEDD8 conjugations to both Cullin1 and Ubc12 in PC3 cells and Ubc12 NEDDylation in an in vitro assay.
Src phosphorylation converts Mdm2 from a ubiquitinating to a neddylating E3 ligase.
Mayo et al., Indianapolis, United States. In Proc Natl Acad Sci U S A, Mar 2015
Here we show that activated c-Src kinase phosphorylates Y281 and Y302 of Mdm2, resulting in an increase in Mdm2 stability and its association with Ubc12, the E2 enzyme of the neddylating complex.
SCCRO3 (DCUN1D3) antagonizes the neddylation and oncogenic activity of SCCRO (DCUN1D1).
Singh et al., New York City, United States. In J Biol Chem, 2015
We found that although SCCRO3 binds to CAND1, cullins, and ROC1, it does not efficiently bind to Ubc12, promote cullin neddylation, or conform to the reaction processivity paradigms, suggesting that SCCRO3 does not have E3 activity.
Neddylation pathway is up-regulated in human intrahepatic cholangiocarcinoma and serves as a potential therapeutic target.
Fan et al., Shanghai, China. In Oncotarget, 2014
Immunohistochemistry of neddylation pathway components in a cohort of 322 cases showed that E1 (NAE1 and UBA3) and E2 (UBC12) enzymes, as well as global NEDD8 conjugation, were upregulated in over 2/3 of human ICC.
Injury-induced immune responses in Hydra.
Galliot et al., Genève, Switzerland. In Semin Immunol, 2014
These regulations point to an enhanced cytoprotection via ROS signaling (Nrf, C/EBP, p62/SQSMT1-l2), TNFR and TLR signaling (TNFR16-like, TRAF2l, TRAF5l, jun, fos-related, SIK2, ATF1/CREB, LRRC28, LRRC40, LRRK2), proteasomal activity (p62/SQSMT1-l1, Ced6/Gulf, NEDD8-conjugating enzyme Ubc12), stress proteins (CRYAB1, CRYAB2, HSP16.2,
Overactivated neddylation pathway as a therapeutic target in lung cancer.
Jia et al., Shanghai, China. In J Natl Cancer Inst, 2014
ubiquitin-conjugating enzyme E2M (UBC12): HR = 13.26,
The covalent modifier Nedd8 is critical for the activation of Smurf1 ubiquitin ligase in tumorigenesis.
Zhang et al., Beijing, China. In Nat Commun, 2013
Smurf1 physically interacts with Nedd8 and Ubc12, forms a Nedd8-thioester intermediate, and then catalyses its own neddylation on multiple lysine residues.
Neddylation pathway regulates T-cell function by targeting an adaptor protein Shc and a protein kinase Erk signaling.
Liu et al., Los Angeles, United States. In Proc Natl Acad Sci U S A, 2013
We found that reduced expression of Ubc12 in CD4(+) T cells led to impaired T-cell receptor/CD28-induced proliferation and cytokine production both in vitro and in vivo, accompanied by reduced Erk activation.
Structural conservation of distinctive N-terminal acetylation-dependent interactions across a family of mammalian NEDD8 ligation enzymes.
Schulman et al., Memphis, United States. In Structure, 2013
We report that the family of human DCN-like (DCNL) co-E3s, which promote ligation of the ubiquitin-like protein NEDD8 to cullin targets, recognizes acetylated N termini of the E2 enzymes UBC12 and UBE2F.
Negative regulation of NEDD8 conjugation pathway by novel molecules and agents for anticancer therapy.
Kamitani et al., Ōsaka, Japan. In Curr Pharm Des, 2012
COP9 signalosome, CAND1, inactive mutant of Ubc12 and NUB1/NUB1L) and clarifies possible strategies for targeting the NEDD8 cascade in cancer cells.
Profiling the cross reactivity of ubiquitin with the Nedd8 activating enzyme by phage display.
Yin et al., Chicago, United States. In Plos One, 2012
Furthermore heptameric peptides derived from the C-terminal sequences of UB variants selected for NAE activation can function as mimics of Nedd8 to form thioester conjugates with NAE and the downstream E2 enzyme Ubc12 in the Nedd8 transfer cascade.
Inhibition of NEDD8-conjugation pathway by novel molecules: potential approaches to anticancer therapy.
Kamitani et al., Ōsaka, Japan. In Mol Oncol, 2012
COP9 signalosome, inactive mutant of Ubc12, and NUB1/NUB1L).
N-terminal acetylation acts as an avidity enhancer within an interconnected multiprotein complex.
Schulman et al., Memphis, United States. In Science, 2011
Here, we found that N-terminal acetylation of the E2 enzyme, Ubc12, dictates distinctive E3-dependent ligation of the ubiquitin-like protein Nedd8 to Cul1.
UBE2M-mediated p27(Kip1) degradation in gemcitabine cytotoxicity.
Pu et al., Kao-hsiung, Taiwan. In Biochem Pharmacol, 2011
Our results demonstrate a role for UBE2M in mediating cytotoxicity of gemcitabine in human urothelial carcinoma cells.
SCCRO (DCUN1D1) is an essential component of the E3 complex for neddylation.
Singh et al., New York City, United States. In J Biol Chem, 2008
SCCRO recruits Ubc12 approximately NEDD8 to the CAND1-Cul1-ROC1 complex but that this is not sufficient to dissociate or overcome the inhibitory effects of CAND1 on cullin neddylation
Structural insights into early events in the conjugation of ubiquitin and ubiquitin-like proteins.
Haas, New Orleans, United States. In Mol Cell, 2007
NMR studies of the SUMO-activating enzyme in complex with Ubc9 (Wang et al., 2007, this issue of Molecular Cell) complement a recent crystal structure of Ubc12 bound to the NEDD8-activating enzyme ternary complex (Huang et al., 2007), elucidating details of the first steps in the conjugation of ubiquitin and ubiquitin-like proteins.
Basis for a ubiquitin-like protein thioester switch toggling E1-E2 affinity.
Schulman et al., Memphis, United States. In Nature, 2007
Here we report the structural analysis of a trapped UBL activation complex for the human NEDD8 pathway, containing NEDD8's heterodimeric E1 (APPBP1-UBA3), two NEDD8s (one thioester-linked to E1, one noncovalently associated for adenylation), a catalytically inactive E2 (Ubc12), and MgATP.
Structural basis for recruitment of Ubc12 by an E2 binding domain in NEDD8's E1.
Schulman et al., Memphis, United States. In Mol Cell, 2005
crystal structure of a complex between the C-terminal domain from NEDD8's heterodimeric E1 (APPBP1-UBA3) and the catalytic core domain of NEDD8's E2 (Ubc12)
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