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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: Ubiquitin, NEDD8, Cullin, SCF, V1a
Papers on Ubc12
Substrates of IAP ubiquitin ligases identified with a designed orthogonal E3 ligase, the NEDDylator.
Wells et al., San Francisco, United States. In Mol Cell, Feb 2013
Here we report a powerful catalytic tagging tool, the NEDDylator, which fuses a NEDD8 E2-conjugating enzyme, Ubc12, to the ubiquitin ligase, XIAP or cIAP1.
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, Feb 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, Feb 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.
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.
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.
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).
E1-E2 interactions in ubiquitin and Nedd8 ligation pathways.
Haas et al., New Orleans, United States. In J Biol Chem, 2012
Truncation of the paralogous domain from the Nedd8 activating enzyme has negligible effect on cognate Ubc12 transthiolation but abrogates E2 specificity toward non-cognate carrier proteins.
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.
The TFIIH subunit Tfb3 regulates cullin neddylation.
Peter et al., Zürich, Switzerland. In Mol Cell, 2011
Instead, ubiquitylation of Rtt101 was dependent on the ubiquitin-conjugating enzyme Ubc4, while efficient neddylation involves the RING domain protein Tfb3, a subunit of the transcription factor TFIIH. Tfb3 also controls Cul3 neddylation and activity in vivo, and physically interacts with Ubc4 and the Nedd8-conjugating enzyme Ubc12 and the Hrt1/Rtt101 complex.
A RING E3-substrate complex poised for ubiquitin-like protein transfer: structural insights into cullin-RING ligases.
Schulman et al., Memphis, United States. In Nat Struct Mol Biol, 2011
Here we address how the RING E3 RBX1 positions NEDD8's E2 (UBC12) and substrate (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) promotes nuclear translocation and assembly of the neddylation E3 complex.
Singh et al., New York City, United States. In J Biol Chem, 2011
SCCRO/DCUN1D1/DCN1 (squamous cell carcinoma-related oncogene/defective in cullin neddylation 1 domain containing 1/defective in cullin neddylation) serves as an accessory E3 in neddylation by binding to cullin and Ubc12 to allow efficient transfer of Nedd8.
Engineering a protein-protein interface using a computationally designed library.
Kuhlman et al., Chapel Hill, United States. In Proc Natl Acad Sci U S A, 2010
Here, we test if these two traditionally alternative, but potentially complementary approaches can be combined to design a variant of the ubiquitin-ligase E6AP that will bind to a nonnatural partner, the NEDD8-conjugating enzyme Ubc12.
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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