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[E1 NEDD8-activating enzyme]-S-[NEDD8 protein]-yl-L-cysteine + [E2 NEDD8-conjugating enzyme]-L-cysteine
[E1 NEDD8-activating enzyme]-L-cysteine + [E2 NEDD8-conjugating enzyme]-S-[NEDD8-protein]-yl-L-cysteine
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[E1 NEDD8-activating enzyme]-S-[NEDD8 protein]-yl-L-cysteine + [E2 NEDD8-conjugating enzyme]-L-cysteine

[E1 NEDD8-activating enzyme]-L-cysteine + [E2 NEDD8-conjugating enzyme]-S-[NEDD8-protein]-yl-L-cysteine
Substrates: -
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[E1 NEDD8-activating enzyme]-S-[NEDD8 protein]-yl-L-cysteine + [E2 NEDD8-conjugating enzyme]-L-cysteine
[E1 NEDD8-activating enzyme]-L-cysteine + [E2 NEDD8-conjugating enzyme]-S-[NEDD8-protein]-yl-L-cysteine
Substrates: -
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[E1 NEDD8-activating enzyme]-S-[NEDD8 protein]-yl-L-cysteine + [E2 NEDD8-conjugating enzyme]-L-cysteine
[E1 NEDD8-activating enzyme]-L-cysteine + [E2 NEDD8-conjugating enzyme]-S-[NEDD8-protein]-yl-L-cysteine
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Substrates: -
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[E1 NEDD8-activating enzyme]-S-[NEDD8 protein]-yl-L-cysteine + [E2 NEDD8-conjugating enzyme]-L-cysteine
[E1 NEDD8-activating enzyme]-L-cysteine + [E2 NEDD8-conjugating enzyme]-S-[NEDD8-protein]-yl-L-cysteine
Substrates: -
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[E1 NEDD8-activating enzyme]-S-[NEDD8 protein]-yl-L-cysteine + [E2 NEDD8-conjugating enzyme]-L-cysteine
[E1 NEDD8-activating enzyme]-L-cysteine + [E2 NEDD8-conjugating enzyme]-S-[NEDD8-protein]-yl-L-cysteine
Substrates: -
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[E1 NEDD8-activating enzyme]-S-[NEDD8 protein]-yl-L-cysteine + [E2 NEDD8-conjugating enzyme]-L-cysteine
[E1 NEDD8-activating enzyme]-L-cysteine + [E2 NEDD8-conjugating enzyme]-S-[NEDD8-protein]-yl-L-cysteine
Substrates: conjugation of NEDD8 to UBC12 requires the involvement of APP-BP1 and UBA3
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[E1 NEDD8-activating enzyme]-S-[NEDD8 protein]-yl-L-cysteine + [E2 NEDD8-conjugating enzyme]-L-cysteine
[E1 NEDD8-activating enzyme]-L-cysteine + [E2 NEDD8-conjugating enzyme]-S-[NEDD8-protein]-yl-L-cysteine
Substrates: -
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[E1 NEDD8-activating enzyme]-S-[NEDD8 protein]-yl-L-cysteine + [E2 NEDD8-conjugating enzyme]-L-cysteine
[E1 NEDD8-activating enzyme]-L-cysteine + [E2 NEDD8-conjugating enzyme]-S-[NEDD8-protein]-yl-L-cysteine
Substrates: -
Products: -
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[E1 NEDD8-activating enzyme]-S-[NEDD8 protein]-yl-L-cysteine + [E2 NEDD8-conjugating enzyme]-L-cysteine
[E1 NEDD8-activating enzyme]-L-cysteine + [E2 NEDD8-conjugating enzyme]-S-[NEDD8-protein]-yl-L-cysteine
Substrates: -
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[E1 NEDD8-activating enzyme]-S-[NEDD8 protein]-yl-L-cysteine + [E2 NEDD8-conjugating enzyme]-L-cysteine
[E1 NEDD8-activating enzyme]-L-cysteine + [E2 NEDD8-conjugating enzyme]-S-[NEDD8-protein]-yl-L-cysteine
Substrates: -
Products: -
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[E1 NEDD8-activating enzyme]-S-[NEDD8 protein]-yl-L-cysteine + [E2 NEDD8-conjugating enzyme]-L-cysteine
[E1 NEDD8-activating enzyme]-L-cysteine + [E2 NEDD8-conjugating enzyme]-S-[NEDD8-protein]-yl-L-cysteine
Substrates: -
Products: -
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[E1 NEDD8-activating enzyme]-S-[NEDD8 protein]-yl-L-cysteine + [E2 NEDD8-conjugating enzyme]-L-cysteine
[E1 NEDD8-activating enzyme]-L-cysteine + [E2 NEDD8-conjugating enzyme]-S-[NEDD8-protein]-yl-L-cysteine
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Substrates: -
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[E1 NEDD8-activating enzyme]-S-[NEDD8 protein]-yl-L-cysteine + [E2 NEDD8-conjugating enzyme]-L-cysteine
[E1 NEDD8-activating enzyme]-L-cysteine + [E2 NEDD8-conjugating enzyme]-S-[NEDD8-protein]-yl-L-cysteine
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additional information

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Substrates: the enzyme participates in neddylation of DNA-dependent protein kinase catalytic subunit
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additional information
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Substrates: RBX2 is specific for UBE2F, which mediates neddylation of the RBX2 partner, cullin 5
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additional information
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Substrates: RBX2 is specific for UBE2F, which mediates neddylation of the RBX2 partner, cullin 5
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additional information
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Substrates: RBX2 is specific for UBE2F, which mediates neddylation of the RBX2 partner, cullin 5
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Substrates: UBC12 is specific for RBX1 and mediates neddylation of RBX1-associated cullins 1, 2, 3 and 4
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Substrates: UBC12 is specific for RBX1 and mediates neddylation of RBX1-associated cullins 1, 2, 3 and 4
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additional information
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Substrates: UBC12 is specific for RBX1 and mediates neddylation of RBX1-associated cullins 1, 2, 3 and 4
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additional information
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Substrates: UBE2M can pair with RBX1 to modulate the neddylation of CUL1, 2, 3, 4A, and 4B. Specifically, UBE2M serves as a stress-inducible protein and a dual E2 for neddylation and ubiquitylation to degrade UBE2F
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additional information
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Substrates: UBE2M can pair with RBX1 to modulate the neddylation of CUL1, 2, 3, 4A, and 4B. Specifically, UBE2M serves as a stress-inducible protein and a dual E2 for neddylation and ubiquitylation to degrade UBE2F
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additional information
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Substrates: UBE2F is very specific to the neddylation of RBX2-related CUL5
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additional information
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Substrates: UBE2F is very specific to the neddylation of RBX2-related CUL5
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additional information
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Substrates: NEDD8 acetylated at K11 is poorly used by the enzymes UBE2F and UBE2M
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additional information
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Substrates: NEDD8 acetylated at K11 is poorly used by the enzymes UBE2F and UBE2M
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additional information
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Substrates: NEDD8 acetylated at K11 is poorly used by the enzymes UBE2F and UBE2M
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additional information
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Substrates: the enzyme UBE2F specifically pairs with RING-box protein 2 to promote cullin 5 neddylation and activation
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additional information
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Substrates: RBX2 associates with the enzyme UBE2F for neddylation of CUL5 at K724
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Substrates: the enzyme UBE2M couples with RBX1 E3 to promote neddylation of cullins 1-4
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[E1 NEDD8-activating enzyme]-S-[NEDD8 protein]-yl-L-cysteine + [E2 NEDD8-conjugating enzyme]-L-cysteine
[E1 NEDD8-activating enzyme]-L-cysteine + [E2 NEDD8-conjugating enzyme]-S-[NEDD8-protein]-yl-L-cysteine
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[E1 NEDD8-activating enzyme]-S-[NEDD8 protein]-yl-L-cysteine + [E2 NEDD8-conjugating enzyme]-L-cysteine

[E1 NEDD8-activating enzyme]-L-cysteine + [E2 NEDD8-conjugating enzyme]-S-[NEDD8-protein]-yl-L-cysteine
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[E1 NEDD8-activating enzyme]-S-[NEDD8 protein]-yl-L-cysteine + [E2 NEDD8-conjugating enzyme]-L-cysteine
[E1 NEDD8-activating enzyme]-L-cysteine + [E2 NEDD8-conjugating enzyme]-S-[NEDD8-protein]-yl-L-cysteine
Substrates: -
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[E1 NEDD8-activating enzyme]-S-[NEDD8 protein]-yl-L-cysteine + [E2 NEDD8-conjugating enzyme]-L-cysteine
[E1 NEDD8-activating enzyme]-L-cysteine + [E2 NEDD8-conjugating enzyme]-S-[NEDD8-protein]-yl-L-cysteine
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[E1 NEDD8-activating enzyme]-S-[NEDD8 protein]-yl-L-cysteine + [E2 NEDD8-conjugating enzyme]-L-cysteine
[E1 NEDD8-activating enzyme]-L-cysteine + [E2 NEDD8-conjugating enzyme]-S-[NEDD8-protein]-yl-L-cysteine
Substrates: -
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[E1 NEDD8-activating enzyme]-S-[NEDD8 protein]-yl-L-cysteine + [E2 NEDD8-conjugating enzyme]-L-cysteine
[E1 NEDD8-activating enzyme]-L-cysteine + [E2 NEDD8-conjugating enzyme]-S-[NEDD8-protein]-yl-L-cysteine
Substrates: -
Products: -
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[E1 NEDD8-activating enzyme]-S-[NEDD8 protein]-yl-L-cysteine + [E2 NEDD8-conjugating enzyme]-L-cysteine
[E1 NEDD8-activating enzyme]-L-cysteine + [E2 NEDD8-conjugating enzyme]-S-[NEDD8-protein]-yl-L-cysteine
Substrates: conjugation of NEDD8 to UBC12 requires the involvement of APP-BP1 and UBA3
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[E1 NEDD8-activating enzyme]-S-[NEDD8 protein]-yl-L-cysteine + [E2 NEDD8-conjugating enzyme]-L-cysteine
[E1 NEDD8-activating enzyme]-L-cysteine + [E2 NEDD8-conjugating enzyme]-S-[NEDD8-protein]-yl-L-cysteine
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[E1 NEDD8-activating enzyme]-S-[NEDD8 protein]-yl-L-cysteine + [E2 NEDD8-conjugating enzyme]-L-cysteine
[E1 NEDD8-activating enzyme]-L-cysteine + [E2 NEDD8-conjugating enzyme]-S-[NEDD8-protein]-yl-L-cysteine
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[E1 NEDD8-activating enzyme]-S-[NEDD8 protein]-yl-L-cysteine + [E2 NEDD8-conjugating enzyme]-L-cysteine
[E1 NEDD8-activating enzyme]-L-cysteine + [E2 NEDD8-conjugating enzyme]-S-[NEDD8-protein]-yl-L-cysteine
Substrates: -
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[E1 NEDD8-activating enzyme]-S-[NEDD8 protein]-yl-L-cysteine + [E2 NEDD8-conjugating enzyme]-L-cysteine
[E1 NEDD8-activating enzyme]-L-cysteine + [E2 NEDD8-conjugating enzyme]-S-[NEDD8-protein]-yl-L-cysteine
Substrates: -
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[E1 NEDD8-activating enzyme]-S-[NEDD8 protein]-yl-L-cysteine + [E2 NEDD8-conjugating enzyme]-L-cysteine
[E1 NEDD8-activating enzyme]-L-cysteine + [E2 NEDD8-conjugating enzyme]-S-[NEDD8-protein]-yl-L-cysteine
Substrates: -
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[E1 NEDD8-activating enzyme]-S-[NEDD8 protein]-yl-L-cysteine + [E2 NEDD8-conjugating enzyme]-L-cysteine
[E1 NEDD8-activating enzyme]-L-cysteine + [E2 NEDD8-conjugating enzyme]-S-[NEDD8-protein]-yl-L-cysteine
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Substrates: -
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[E1 NEDD8-activating enzyme]-S-[NEDD8 protein]-yl-L-cysteine + [E2 NEDD8-conjugating enzyme]-L-cysteine
[E1 NEDD8-activating enzyme]-L-cysteine + [E2 NEDD8-conjugating enzyme]-S-[NEDD8-protein]-yl-L-cysteine
Substrates: -
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additional information

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Substrates: UBE2M can pair with RBX1 to modulate the neddylation of CUL1, 2, 3, 4A, and 4B. Specifically, UBE2M serves as a stress-inducible protein and a dual E2 for neddylation and ubiquitylation to degrade UBE2F
Products: -
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additional information
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Substrates: UBE2M can pair with RBX1 to modulate the neddylation of CUL1, 2, 3, 4A, and 4B. Specifically, UBE2M serves as a stress-inducible protein and a dual E2 for neddylation and ubiquitylation to degrade UBE2F
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additional information
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Substrates: UBE2F is very specific to the neddylation of RBX2-related CUL5
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additional information
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Substrates: UBE2F is very specific to the neddylation of RBX2-related CUL5
Products: -
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Atherosclerosis
Identification of candidate targets for the diagnosis and treatment of atherosclerosis by bioinformatics analysis.
Breast Neoplasms
UBC12-mediated SREBP-1 neddylation worsens metastatic tumor prognosis.
Carcinoma
Control of cell proliferation via elevated NEDD8 conjugation in oral squamous cell carcinoma.
Carcinoma
Improvement of Oral Bioavailability of Pyrazolo-Pyridone Inhibitors of the Interaction of DCN1/2 and UBE2M.
Carcinoma
NEDD8-conjugating enzyme UBC12 as a novel therapeutic target in esophageal squamous cell carcinoma.
Carcinoma
UBE2M-mediated p27(Kip1) degradation in gemcitabine cytotoxicity.
Carcinoma, Hepatocellular
UBC12-mediated SREBP-1 neddylation worsens metastatic tumor prognosis.
Carcinoma, Hepatocellular
UBE2M promotes cell proliferation via the ?-catenin/cyclin D1 signaling in hepatocellular carcinoma.
Carcinoma, Squamous Cell
Improvement of Oral Bioavailability of Pyrazolo-Pyridone Inhibitors of the Interaction of DCN1/2 and UBE2M.
Cholangiocarcinoma
Knockdown of Nedd8?conjugating enzyme UBE2M suppresses the proliferation and induces the apoptosis of intrahepatic cholangiocarcinoma cells.
Colorectal Neoplasms
The covalent modifier Nedd8 is critical for the activation of Smurf1 ubiquitin ligase in tumorigenesis.
Endometrial Neoplasms
MLN4924 inhibits cell proliferation by targeting the activated neddylation pathway in endometrial carcinoma.
Esophageal Squamous Cell Carcinoma
NEDD8-conjugating enzyme UBC12 as a novel therapeutic target in esophageal squamous cell carcinoma.
Hypersensitivity
Neddylation promotes ubiquitylation and release of Ku from DNA-damage sites.
Infections
RNF111-facilitated neddylation potentiates cGAS-mediated antiviral innate immune response.
Infections
Treatment of Yersinia similis with the cationic lipid DOTAP enhances adhesion to and invasion into intestinal epithelial cells - A proof-of-principle study.
Kidney Neoplasms
A first-in-class inhibitor, MLN4924 (pevonedistat), induces cell-cycle arrest, senescence, and apoptosis in human renal cell carcinoma by suppressing UBE2M-dependent neddylation modification.
Lung Neoplasms
Induction of NEDD8-conjugating enzyme E2 UBE2F by platinum protects lung cancer cells from apoptosis and confers to platinum-insensitivity.
Lung Neoplasms
Neddylation E2 UBE2F promotes the survival of lung cancer cells by activating CRL5 to degrade NOXA via the K11 linkage.
Lung Neoplasms
UBE2M Is a Stress-Inducible Dual E2 for Neddylation and Ubiquitylation that Promotes Targeted Degradation of UBE2F.
Lung Neoplasms
Validation of NEDD8-conjugating enzyme UBC12 as a new therapeutic target in lung cancer.
Lymphatic Metastasis
UBC12-mediated SREBP-1 neddylation worsens metastatic tumor prognosis.
Neoplasm Metastasis
UBC12-mediated SREBP-1 neddylation worsens metastatic tumor prognosis.
Neoplasms
Correlation of histopathologic characteristics to protein expression and function in malignant melanoma.
Neoplasms
Knockdown of Nedd8?conjugating enzyme UBE2M suppresses the proliferation and induces the apoptosis of intrahepatic cholangiocarcinoma cells.
Neoplasms
MLN4924 (Pevonedistat), a protein neddylation inhibitor, suppresses proliferation and migration of human clear cell renal cell carcinoma.
Neoplasms
Neddylation E2 UBE2F promotes the survival of lung cancer cells by activating CRL5 to degrade NOXA via the K11 linkage.
Neoplasms
Negative Regulation of NEDD8 Conjugation Pathway by Novel Molecules and Agents for Anticancer Therapy.
Neoplasms
NPRL2 reduces the niraparib sensitivity of castration-resistant prostate cancer via interacting with UBE2M and enhancing neddylation.
Neoplasms
Suppression of glioblastoma by targeting the overactivated protein neddylation pathway.
Neoplasms
Targeting neddylation E2s: a novel therapeutic strategy in cancer.
Neoplasms
The covalent modifier Nedd8 is critical for the activation of Smurf1 ubiquitin ligase in tumorigenesis.
Neoplasms
UBC12-mediated SREBP-1 neddylation worsens metastatic tumor prognosis.
Neoplasms
UBE2M promotes cell proliferation via the ?-catenin/cyclin D1 signaling in hepatocellular carcinoma.
Neoplasms
UBE2M-mediated p27(Kip1) degradation in gemcitabine cytotoxicity.
Pancreatitis
Neddylation pathway alleviates chronic pancreatitis by reducing HIF1?-CCL5-dependent macrophage infiltration.
Prostatic Neoplasms
Flavokawain B targets protein neddylation for enhancing the anti-prostate cancer effect of Bortezomib via Skp2 degradation.
Prostatic Neoplasms
Gartanin is a novel NEDDylation inhibitor for induction of Skp2 degradation, FBXW2 expression, and autophagy.
Prostatic Neoplasms
NPRL2 reduces the niraparib sensitivity of castration-resistant prostate cancer via interacting with UBE2M and enhancing neddylation.
ring-type e3 ubiquitin transferase deficiency
RNF111-facilitated neddylation potentiates cGAS-mediated antiviral innate immune response.
Squamous Cell Carcinoma of Head and Neck
The Nedd8-activating enzyme inhibitor MLN4924 (TAK-924/Pevonedistat) induces apoptosis via c-Myc-Noxa axis in head and neck squamous cell carcinoma.
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malfunction

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enzyme depletion results in decreased DNA-dependent protein kinase catalytic subunit neddylation
malfunction
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knocking down Ube2m leads to decreased Nedd8-ylation of endogenous cullins 1-4, and a marginal increase in Nedd8-modified cullin 5 By contrast, knocking down Ube2f virtually eliminates the presence of Nedd8-ylated cullin 5, and has no effect on the levels of Nedd8-modified cullins 1-4
malfunction
regulatory T cell Ube2m-enzyme deficiency causes obvious inflammation disorders but with phenotype severity much less than that seen in regulatory T cell Rbx1-deficient mice
malfunction
enzyme UBE2M is highly associated with obesity and obesity-related metabolic diseases. Mechanically, UBE2M promotes TRIM21 neddylation to enhance TRIM21-mediated von Hippel-Lindau protein ubiquitylation
malfunction
UBE2M inhibition induces cell cycle arrest and apoptosis or senescence
malfunction
UBE2F inhibition induces apoptosis
malfunction
liver-specific enzyme knockout attenuates steatosis and tumorigenesis induced by Pten loss in an mTORC1-dependent manner, suggesting a causal role of the enzyme in liver tumorigenesis
malfunction
enzyme UBE2M deficiency in macrophages attenuates inflammation and organ injuries caused by Escherichia coli infection without impairing bacterial clearance
metabolism

the N-terminal extension of Ubc12 is a selective peptide motif that optimally recruits NEDD8 E1 for the NEDD8 transfer cascade and plays an important role in mitogenesis
metabolism
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the enzyme incorporates with E3 neddylation ligase to induce cullin-RING ligase-5 neddylation, leading to activation of cullin-RING ligase-5 E3 to promote NOXA polyubiquitylation via K11 linkage for proteasomal degradation
metabolism
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UBC12 pairs with RBX1/ROC1 to regulate the neddylation of cullin 1, 2, 3, 4a, 4b and 7, while UBE2F pairs with RBX2/ROC2 to regulate the neddylation of cullin 5
physiological function

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UBE2M is a dual E2 for targeted ubiquitylation and degradation of UBE2F, acting as a neddylation E2 to activate cullin 3-Keap1 E3 under physiological condition, but as an ubiquitylation E2 for Parkin-DJ-1 E3 under stressed conditions. UBE2M-induced UBE2F degradation leads to CRL5 inactivation and subsequent NOXA accumulation to suppress the growth of lung cancer cells
physiological function
the Ube2m-Rbx1 axis is specifically required for intrinsic regulatory processes in regulatory T cells
physiological function
UBE2M influences tumor growth by modulating several biological responses of tumor cells, such as DNA-damage response, cell cycle arrest, apoptosis, or senescence
physiological function
the enzyme plays an important role in tumor progression
physiological function
UBE2F promotes the degradation of NOXA and then inhibits apoptosis and induces tumor growth
physiological function
in cell culture, enzyme depletion inactivates mTORC1, inhibiting cell cycle progression, cell growth and inducing autophagy. Mechanistically, the enzyme cooperates with E3 ligase SAG in neddylation of RHEB at K169 to enhance its lysosome localization and GTP-binding affinity
physiological function
enzyme overexpression significantly enhances the yes-associated protein 1-driven promoter activity and functions
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Monda, J.; Scott, D.; Miller, D.; Lydeard, J.; King, D.; Harper, J.; Bennett, E.; Schulman, B.
Structural conservation of distinctive N-terminal acetylation-dependent interactions across a family of mammalian NEDD8 ligation enzymes
Structure
21
42-53
2013
Homo sapiens (P61081), Homo sapiens (Q969M7), Homo sapiens
brenda
Zhang, S.; Sun, Y.
Cullin RING Ligase 5 (CRL-5) neddylation activation and biological functions
Adv. Exp. Med. Biol.
1217
261-283
2020
Homo sapiens
brenda
Guo, Z.; Wang, S.; Xie, Y.; Han, Y.; Hu, S.; Guan, H.; Xie, D.; Bai, C.; Liu, X.; Gu, Y.; Zhou, P.K.; Ma, T.
HUWE1-dependent DNA-PKcs neddylation modulates its autophosphorylation in DNA damage response
Cell Death Dis.
11
400
2020
Homo sapiens
brenda
Yin, L.; Xue, Y.; Shang, Q.; Zhu, H.; Liu, M.; Liu, Y.; Hu, Q.
Pharmaceutical inhibition of neddylation as promising treatments for various cancers
Curr. Top. Med. Chem.
19
1059-1069
2019
Homo sapiens (P61081)
brenda
Li, L.; Kang, J.; Zhang, W.; Cai, L.; Wang, S.; Liang, Y.; Jiang, Y.; Liu, X.; Zhang, Y.; Ruan, H.; Chen, G.; Wang, M.; Jia, L.
Validation of NEDD8-conjugating enzyme UBC12 as a new therapeutic target in lung cancer
EBioMedicine
45
81-91
2019
Homo sapiens
brenda
Osaka, F.; Kawasaki, H.; Aida, N.; Saeki, M.; Chiba, T.; Kawashima, S.; Tanaka, K.; Kato, S.
A new NEDD8-ligating system for cullin-4A
Genes Dev.
12
2263-2268
1998
Homo sapiens (P61081)
brenda
Gong, L.; Yeh, E.
Identification of the activating and conjugating enzymes of the NEDD8 conjugation pathway
J. Biol. Chem.
274
12036-12042
1999
Homo sapiens (P61081), Homo sapiens
brenda
Huang, D.T.; Ayrault, O.; Hunt, H.W.; Taherbhoy, A.M.; Duda, D.M.; Scott, D.C.; Borg, L.A.; Neale, G.; Murray, P.J.; Roussel, M.F.; Schulman, B.A.
E2-RING expansion of the NEDD8 cascade confers specificity to cullin modification
Mol. Cell
33
483-495
2009
Mus musculus
brenda
Zhou, W.; Xu, J.; Tan, M.; Li, H.; Li, H.; Wei, W.; Sun, Y.
UBE2M is a stress-inducible dual E2 for neddylation and ubiquitylation that promotes targeted degradation of UBE2F
Mol. Cell
70
1008-1024
2018
Homo sapiens
brenda
Huang, D.; Miller, D.; Mathew, R.; Cassell, R.; Holton, J.; Roussel, M.; Schulman, B.
A unique E1-E2 interaction required for optimal conjugation of the ubiquitin-like protein NEDD8
Nat. Struct. Mol. Biol.
11
927-935
2004
Homo sapiens (P61081)
brenda
Chen, Y.F.; Liu, R.Z.; Ying, W.W.; Yang, Y.N.; Xiang, S.F.; Shao, X.J.; Cao, J.; Zhang, Y.Q.; Yang, B.; He, Q.J.; Ying, M.D.
Arctigenin impairs UBC12 enzyme activity and cullin neddylation to attenuate cancer cells
Acta Pharmacol. Sin.
44
661-669
2023
Homo sapiens (P61081)
brenda
Zhou, L.; Lin, X.; Zhu, J.; Zhang, L.; Chen, S.; Yang, H.; Jia, L.; Chen, B.
NEDD8-conjugating enzyme E2s critical targets for cancer therapy
Cell Death Discov.
9
23
2023
Homo sapiens (P61081), Homo sapiens (Q969M7)
brenda
Kienle, S.M.; Schneider, T.; Bernecker, C.; Bracker, J.; Marx, A.; Kovermann, M.; Scheffner, M.; Stuber, K.
Biochemical and structural consequences of NEDD8 acetylation
ChemBioChem
25
e202400478
2024
Homo sapiens, Homo sapiens (P61081), Homo sapiens (Q969M7)
brenda
Baek, K.; Scott, D.C.; Schulman, B.A.
NEDD8 and ubiquitin ligation by cullin-RING E3 ligases
Curr. Opin. Struct. Biol.
67
101-109
2021
Homo sapiens (P61081)
brenda
Zhang, F.; Xiong, X.; Li, Z.; Wang, H.; Wang, W.; Zhao, Y.; Sun, Y.
RHEB neddylation by the UBE2F-SAG axis enhances mTORC1 activity and aggravates liver tumorigenesis
EMBO J.
44
1185-1219
2025
Homo sapiens (Q969M7)
brenda
Chen, M.; Liu, Y.; Zuo, M.; Guo, C.; Du, Y.; Xu, H.; Liu, B.; Li, M.; Xiao, W.; Yu, G.
NEDD8 enhances Hippo signaling by mediating YAP1 neddylation
J. Biol. Chem.
300
107512
2024
Danio rerio (F1QMF9)
brenda
Wen, X.; Bai, S.; Xiong, G.; Xiu, H.; Li, J.; Yang, J.; Yu, Q.; Li, B.; Hu, R.; Cao, L.; Cai, Z.; Zhang, S.; Zhang, G.
Inhibition of the neddylation E2 enzyme UBE2M in macrophages protects against E.coli-induced sepsis
J. Biol. Chem.
301
108085
2025
Mus musculus (P61082)
brenda
Zhou, L.; Dong, C.; Xu, Z.; Wang, X.; Zhang, L.; Chen, S.; Chen, J.; Zhu, Y.
NEDD8-conjugating enzyme E2 UBE2F confers radiation resistance by protecting lung cancer cells from apoptosis
J. Zhejiang Univ. Sci. B
22
959-965
2021
Homo sapiens (Q969M7)
brenda
Lumpkin, R.J.; Ahmad, A.S.; Blake, R.; Condon, C.J.; Komives, E.A.
The mechanism of NEDD8 activation of CUL5 ubiquitin E3 ligases
Mol. Cell. Proteomics
20
100019
2021
Homo sapiens (Q969M7)
brenda
Wu, D.; Li, H.; Liu, M.; Qin, J.; Sun, Y.
The Ube2m-Rbx1 neddylation-Cullin-RING-Ligase proteins are essential for the maintenance of regulatory T cell fitness
Nat. Commun.
13
3021
2022
Mus musculus (P61082)
brenda
Zhang, S.; Yu, Q.; Li, Z.; Zhao, Y.; Sun, Y.
Protein neddylation and its role in health and diseases
Signal Transduct. Target. Ther.
9
85
2024
Homo sapiens (P61081), Homo sapiens (Q969M7)
brenda