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Information on EC 2.3.2.32 - cullin-RING-type E3 NEDD8 transferase
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EC Tree
2.3.2.32 cullin-RING-type E3 NEDD8 transferaseIUBMB Comments
Some RING-type E3 ubiquitin transferase (EC 2.3.2.27) are not able to bind a substrate protein directly. Instead, they form a complex with a cullin scaffold protein and a substrate recognition module, which is named CRL for Cullin-RING-Ligase. The cullin protein needs to be activated by the ubiquitin-like protein NEDD8 in a process known as neddylation. The transfer of NEDD8 from a NEDD8-specific E2 enzyme onto the cullin protein is a secondary function of the RING-type E3 ubiquitin transferase in the CRL complex. The process requires auxiliary factors that belong to the DCN1 (defective in cullin neddylation 1) family.
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The enzyme appears in viruses and cellular organisms
Reaction Schemes
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[E2 NEDD8-conjugating enzyme]-S-[NEDD8-protein]-yl-L-cysteine
+
[cullin]-L-lysine
=
[E2 NEDD8-conjugating enzyme]-L-cysteine
+
[cullin]-N6-[NEDD8-protein]-yl-L-lysine
Synonyms
sccro, dcun1d1, cullin-2, rbx-1, dcn-1, dcn1p, dcun1d5, dcnl5, nedd8 e3 ligase, cullin 2-rbx1 e3 ligase, 
more
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SYNONYM 
ORGANISM
UNIPROT
COMMENTARY 
LITERATURE
Dcn1
DCUN1D1
RBX1
SCCRO
RBX1
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REACTION
REACTION DIAGRAM
COMMENTARY
ORGANISM
UNIPROT
LITERATURE
[E2 NEDD8-conjugating enzyme]-S-[NEDD8-protein]-yl-L-cysteine + [cullin]-L-lysine = [E2 NEDD8-conjugating enzyme]-L-cysteine + [cullin]-N6-[NEDD8-protein]-yl-L-lysine
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PATHWAY SOURCE
PATHWAYS
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SYSTEMATIC NAME
IUBMB Comments
[E2 NEDD8-conjugating enzyme]-S-[NEDD8-protein]-yl-L-cysteine:[cullin] [NEDD8-protein] transferase (isopeptide bond-forming; RING-type)
Some RING-type E3 ubiquitin transferase (EC 2.3.2.27) are not able to bind a substrate protein directly. Instead, they form a complex with a cullin scaffold protein and a substrate recognition module, which is named CRL for Cullin-RING-Ligase. The cullin protein needs to be activated by the ubiquitin-like protein NEDD8 in a process known as neddylation. The transfer of NEDD8 from a NEDD8-specific E2 enzyme onto the cullin protein is a secondary function of the RING-type E3 ubiquitin transferase in the CRL complex. The process requires auxiliary factors that belong to the DCN1 (defective in cullin neddylation 1) family.
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SUBSTRATE
PRODUCT
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate)
(Substrate)
LITERATURE
(Substrate)
(Substrate)
COMMENTARY
(Product)
(Product)
LITERATURE
(Product)
(Product)
Reversibility
r=reversible
ir=irreversible
?=not specified
r=reversible
ir=irreversible
?=not specified
[E2 NEDD8-conjugating enzyme Ubc12]-S-[NEDD8-protein]-yl-L-cysteine + [cullin]-L-lysine
[E2 NEDD8-conjugating enzyme Ubc12]-L-cysteine + [cullin]-N6-[NEDD8-protein]-yl-L-lysine
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[E2 NEDD8-conjugating enzyme]-S-[NEDD8-protein]-yl-L-cysteine + [cullin 1]-L-lysine
[E2 NEDD8-conjugating enzyme]-L-cysteine + [cullin 1]-N6-[NEDD8-protein]-yl-L-lysine
[E2 NEDD8-conjugating enzyme]-S-[NEDD8-protein]-yl-L-cysteine + [cullin 1]-L-lysine720
[E2 NEDD8-conjugating enzyme]-L-cysteine + [cullin 1]-N6-[NEDD8-protein]-yl-L-lysine720
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[E2 NEDD8-conjugating enzyme]-S-[NEDD8-protein]-yl-L-cysteine + [cullin 2]-L-lysine
[E2 NEDD8-conjugating enzyme]-L-cysteine + [cullin 2]-N6-[NEDD8-protein]-yl-L-lysine
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[E2 NEDD8-conjugating enzyme]-S-[NEDD8-protein]-yl-L-cysteine + [cullin 3]-L-lysine
[E2 NEDD8-conjugating enzyme]-L-cysteine + [cullin 3]-N6-[NEDD8-protein]-yl-L-lysine
[E2 NEDD8-conjugating enzyme]-S-[NEDD8-protein]-yl-L-cysteine + [cullin 4]-L-lysine
[E2 NEDD8-conjugating enzyme]-L-cysteine + [cullin 4]-N6-[NEDD8-protein]-yl-L-lysine
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[E2 NEDD8-conjugating enzyme]-S-[NEDD8-protein]-yl-L-cysteine + [cullin Cdc53]-L-lysine
[E2 NEDD8-conjugating enzyme]-L-cysteine + [cullin Cdc53]-N6-[NEDD8-protein]-yl-L-lysine
[E2 NEDD8-conjugating enzyme]-S-[NEDD8-protein]-yl-L-cysteine + [cullin-1]-L-lysine
[E2 NEDD8-conjugating enzyme]-L-cysteine + [cullin-1]-N6-[NEDD8-protein]-yl-L-lysine
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[E2 NEDD8-conjugating enzyme]-S-[NEDD8-protein]-yl-L-cysteine + [cullin]-L-lysine
[E2 NEDD8-conjugating enzyme]-L-cysteine + [cullin]-N6-[NEDD8-protein]-yl-L-lysine
[E2 NEDD8-conjugating enzyme]-S-[NEDD8-protein]-yl-L-cysteine + [cullin 1]-L-lysine
[E2 NEDD8-conjugating enzyme]-L-cysteine + [cullin 1]-N6-[NEDD8-protein]-yl-L-lysine
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[E2 NEDD8-conjugating enzyme]-S-[NEDD8-protein]-yl-L-cysteine + [cullin 1]-L-lysine
[E2 NEDD8-conjugating enzyme]-L-cysteine + [cullin 1]-N6-[NEDD8-protein]-yl-L-lysine
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[E2 NEDD8-conjugating enzyme]-S-[NEDD8-protein]-yl-L-cysteine + [cullin 1]-L-lysine
[E2 NEDD8-conjugating enzyme]-L-cysteine + [cullin 1]-N6-[NEDD8-protein]-yl-L-lysine
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[E2 NEDD8-conjugating enzyme]-S-[NEDD8-protein]-yl-L-cysteine + [cullin 3]-L-lysine
[E2 NEDD8-conjugating enzyme]-L-cysteine + [cullin 3]-N6-[NEDD8-protein]-yl-L-lysine
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[E2 NEDD8-conjugating enzyme]-S-[NEDD8-protein]-yl-L-cysteine + [cullin 3]-L-lysine
[E2 NEDD8-conjugating enzyme]-L-cysteine + [cullin 3]-N6-[NEDD8-protein]-yl-L-lysine
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[E2 NEDD8-conjugating enzyme]-S-[NEDD8-protein]-yl-L-cysteine + [cullin Cdc53]-L-lysine
[E2 NEDD8-conjugating enzyme]-L-cysteine + [cullin Cdc53]-N6-[NEDD8-protein]-yl-L-lysine
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[E2 NEDD8-conjugating enzyme]-S-[NEDD8-protein]-yl-L-cysteine + [cullin Cdc53]-L-lysine
[E2 NEDD8-conjugating enzyme]-L-cysteine + [cullin Cdc53]-N6-[NEDD8-protein]-yl-L-lysine
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[E2 NEDD8-conjugating enzyme]-S-[NEDD8-protein]-yl-L-cysteine + [cullin Cdc53]-L-lysine
[E2 NEDD8-conjugating enzyme]-L-cysteine + [cullin Cdc53]-N6-[NEDD8-protein]-yl-L-lysine
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[E2 NEDD8-conjugating enzyme]-S-[NEDD8-protein]-yl-L-cysteine + [cullin Cdc53]-L-lysine
[E2 NEDD8-conjugating enzyme]-L-cysteine + [cullin Cdc53]-N6-[NEDD8-protein]-yl-L-lysine
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[E2 NEDD8-conjugating enzyme]-S-[NEDD8-protein]-yl-L-cysteine + [cullin]-L-lysine
[E2 NEDD8-conjugating enzyme]-L-cysteine + [cullin]-N6-[NEDD8-protein]-yl-L-lysine
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[E2 NEDD8-conjugating enzyme]-S-[NEDD8-protein]-yl-L-cysteine + [cullin]-L-lysine
[E2 NEDD8-conjugating enzyme]-L-cysteine + [cullin]-N6-[NEDD8-protein]-yl-L-lysine
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[E2 NEDD8-conjugating enzyme]-S-[NEDD8-protein]-yl-L-cysteine + [cullin]-L-lysine
[E2 NEDD8-conjugating enzyme]-L-cysteine + [cullin]-N6-[NEDD8-protein]-yl-L-lysine
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[E2 NEDD8-conjugating enzyme]-S-[NEDD8-protein]-yl-L-cysteine + [cullin]-L-lysine
[E2 NEDD8-conjugating enzyme]-L-cysteine + [cullin]-N6-[NEDD8-protein]-yl-L-lysine
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additional information
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ALF4 binds to the enzyme and inhibits the activity of SCFTIR1, an E3 ligase responsible for degradation of the Aux/IAA transcriptional repressors
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additional information
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Rbx1 is a subunit of the related SCF (Skp1-Cdc53/Cul1-F-box protein) and von Hippel-Lindau (VHL) tumor suppressor (elongin BC-Cul2-VHL) E3 ubiquitin ligase complexes, where it functions as a component of Cdc53/Rbx1 and Cul2/ Rbx1 modules that activate ubiquitination of target proteins by the E2 ubiquitin-conjugating enzymes Cdc34 and Ubc5
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additional information
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the NEDD8 conjugating enzyme UBE2M binds specifically to RBX1
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additional information
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conjugation of RBX1 to NEDD8 substantially stimulates the reaction, by nearly 2000fold, activating both substrate-priming and chain-elongation reactions. Presence of NEDD8 coordinates ubiquitin ligation assembly
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additional information
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Ubc12, a NEDD8-specific E2 conjugating enzyme, is a substrate for auto-neddylation. Protease SENP8/DEN1 counteracts Ubc12 autoneddylation, and aberrant neddylation of Ubc12 and other NEDD8 conjugation pathway components is observed in SENP8-deficient cells
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additional information
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the enzyme Hrt1 is a RING-type E3 for Rub1 ligation to Cdc53
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NATURAL SUBSTRATE
NATURAL PRODUCT
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate)
(Substrate)
LITERATURE
(Substrate)
(Substrate)
COMMENTARY
(Product)
(Product)
LITERATURE
(Product)
(Product)
REVERSIBILITY
r=reversible
ir=irreversible
?=not specified
r=reversible
ir=irreversible
?=not specified
[E2 NEDD8-conjugating enzyme]-S-[NEDD8-protein]-yl-L-cysteine + [cullin 1]-L-lysine
[E2 NEDD8-conjugating enzyme]-L-cysteine + [cullin 1]-N6-[NEDD8-protein]-yl-L-lysine
[E2 NEDD8-conjugating enzyme]-S-[NEDD8-protein]-yl-L-cysteine + [cullin 1]-L-lysine720
[E2 NEDD8-conjugating enzyme]-L-cysteine + [cullin 1]-N6-[NEDD8-protein]-yl-L-lysine720
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?
[E2 NEDD8-conjugating enzyme]-S-[NEDD8-protein]-yl-L-cysteine + [cullin 2]-L-lysine
[E2 NEDD8-conjugating enzyme]-L-cysteine + [cullin 2]-N6-[NEDD8-protein]-yl-L-lysine
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?
[E2 NEDD8-conjugating enzyme]-S-[NEDD8-protein]-yl-L-cysteine + [cullin 3]-L-lysine
[E2 NEDD8-conjugating enzyme]-L-cysteine + [cullin 3]-N6-[NEDD8-protein]-yl-L-lysine
[E2 NEDD8-conjugating enzyme]-S-[NEDD8-protein]-yl-L-cysteine + [cullin 4]-L-lysine
[E2 NEDD8-conjugating enzyme]-L-cysteine + [cullin 4]-N6-[NEDD8-protein]-yl-L-lysine
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?
[E2 NEDD8-conjugating enzyme]-S-[NEDD8-protein]-yl-L-cysteine + [cullin Cdc53]-L-lysine
[E2 NEDD8-conjugating enzyme]-L-cysteine + [cullin Cdc53]-N6-[NEDD8-protein]-yl-L-lysine
[E2 NEDD8-conjugating enzyme]-S-[NEDD8-protein]-yl-L-cysteine + [cullin-1]-L-lysine
[E2 NEDD8-conjugating enzyme]-L-cysteine + [cullin-1]-N6-[NEDD8-protein]-yl-L-lysine
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?
[E2 NEDD8-conjugating enzyme]-S-[NEDD8-protein]-yl-L-cysteine + [cullin]-L-lysine
[E2 NEDD8-conjugating enzyme]-L-cysteine + [cullin]-N6-[NEDD8-protein]-yl-L-lysine
additional information
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the enzyme Hrt1 is a RING-type E3 for Rub1 ligation to Cdc53
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[E2 NEDD8-conjugating enzyme]-S-[NEDD8-protein]-yl-L-cysteine + [cullin 1]-L-lysine
[E2 NEDD8-conjugating enzyme]-L-cysteine + [cullin 1]-N6-[NEDD8-protein]-yl-L-lysine
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[E2 NEDD8-conjugating enzyme]-S-[NEDD8-protein]-yl-L-cysteine + [cullin 1]-L-lysine
[E2 NEDD8-conjugating enzyme]-L-cysteine + [cullin 1]-N6-[NEDD8-protein]-yl-L-lysine
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[E2 NEDD8-conjugating enzyme]-S-[NEDD8-protein]-yl-L-cysteine + [cullin 1]-L-lysine
[E2 NEDD8-conjugating enzyme]-L-cysteine + [cullin 1]-N6-[NEDD8-protein]-yl-L-lysine
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?
[E2 NEDD8-conjugating enzyme]-S-[NEDD8-protein]-yl-L-cysteine + [cullin 3]-L-lysine
[E2 NEDD8-conjugating enzyme]-L-cysteine + [cullin 3]-N6-[NEDD8-protein]-yl-L-lysine
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?
[E2 NEDD8-conjugating enzyme]-S-[NEDD8-protein]-yl-L-cysteine + [cullin 3]-L-lysine
[E2 NEDD8-conjugating enzyme]-L-cysteine + [cullin 3]-N6-[NEDD8-protein]-yl-L-lysine
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?
[E2 NEDD8-conjugating enzyme]-S-[NEDD8-protein]-yl-L-cysteine + [cullin Cdc53]-L-lysine
[E2 NEDD8-conjugating enzyme]-L-cysteine + [cullin Cdc53]-N6-[NEDD8-protein]-yl-L-lysine
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?
[E2 NEDD8-conjugating enzyme]-S-[NEDD8-protein]-yl-L-cysteine + [cullin Cdc53]-L-lysine
[E2 NEDD8-conjugating enzyme]-L-cysteine + [cullin Cdc53]-N6-[NEDD8-protein]-yl-L-lysine
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?
[E2 NEDD8-conjugating enzyme]-S-[NEDD8-protein]-yl-L-cysteine + [cullin Cdc53]-L-lysine
[E2 NEDD8-conjugating enzyme]-L-cysteine + [cullin Cdc53]-N6-[NEDD8-protein]-yl-L-lysine
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[E2 NEDD8-conjugating enzyme]-S-[NEDD8-protein]-yl-L-cysteine + [cullin Cdc53]-L-lysine
[E2 NEDD8-conjugating enzyme]-L-cysteine + [cullin Cdc53]-N6-[NEDD8-protein]-yl-L-lysine
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?
[E2 NEDD8-conjugating enzyme]-S-[NEDD8-protein]-yl-L-cysteine + [cullin]-L-lysine
[E2 NEDD8-conjugating enzyme]-L-cysteine + [cullin]-N6-[NEDD8-protein]-yl-L-lysine
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?
[E2 NEDD8-conjugating enzyme]-S-[NEDD8-protein]-yl-L-cysteine + [cullin]-L-lysine
[E2 NEDD8-conjugating enzyme]-L-cysteine + [cullin]-N6-[NEDD8-protein]-yl-L-lysine
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[E2 NEDD8-conjugating enzyme]-S-[NEDD8-protein]-yl-L-cysteine + [cullin]-L-lysine
[E2 NEDD8-conjugating enzyme]-L-cysteine + [cullin]-N6-[NEDD8-protein]-yl-L-lysine
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?
[E2 NEDD8-conjugating enzyme]-S-[NEDD8-protein]-yl-L-cysteine + [cullin]-L-lysine
[E2 NEDD8-conjugating enzyme]-L-cysteine + [cullin]-N6-[NEDD8-protein]-yl-L-lysine
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DISEASE
TITLE OF PUBLICATION
LINK TO PUBMED
Adenocarcinoma
SCCRO expression correlates with invasive progression in bronchioloalveolar carcinoma.
Adenocarcinoma, Bronchiolo-Alveolar
SCCRO expression correlates with invasive progression in bronchioloalveolar carcinoma.
Adrenocortical Adenoma
Squamous cell carcinoma-related oncogene is highly expressed in developing, normal, and adenomatous adrenal tissue but not in aggressive adrenocortical carcinomas.
Adrenocortical Carcinoma
Squamous cell carcinoma-related oncogene is highly expressed in developing, normal, and adenomatous adrenal tissue but not in aggressive adrenocortical carcinomas.
Breast Neoplasms
Widespread Alternative Splicing Changes in Metastatic Breast Cancer Cells.
Carcinoma
Association of ring box-1 protein overexpression with clinicopathologic prognostic parameters in prostate carcinoma.
Carcinoma
Coamplification and Cooperation: Toward Identifying Biologically Relevant Oncogenes.
Carcinoma
Expression of DCUN1D1 in laryngeal squamous cell carcinoma and its inhibiting effect on TU-177 cells after interfered by RNA.
Carcinoma
Immunohistochemical Expression of DCUN1D1 in Non-small Cell Lung Carcinoma: Its Relation to Brain Metastasis.
Carcinoma
MicroRNA-195 inhibits growth and invasion of laryngeal carcinoma cells by directly targeting DCUN1D1.
Carcinoma
SCCRO (DCUN1D1) induces extracellular matrix invasion by activating matrix metalloproteinase 2.
Carcinoma
Squamous cell carcinoma related oncogene regulates angiogenesis through vascular endothelial growth factor-A.
Carcinoma
The ubiquitin-associated (UBA) domain of SCCRO/DCUN1D1 protein serves as a feedback regulator of biochemical and oncogenic activity.
Carcinoma, Non-Small-Cell Lung
Immunohistochemical Expression of DCUN1D1 in Non-small Cell Lung Carcinoma: Its Relation to Brain Metastasis.
Carcinoma, Renal Cell
An integrated computational approach can classify VHL missense mutations according to risk of clear cell renal carcinoma.
Carcinoma, Squamous Cell
Coamplification and Cooperation: Toward Identifying Biologically Relevant Oncogenes.
Carcinoma, Squamous Cell
Squamous cell carcinoma related oncogene regulates angiogenesis through vascular endothelial growth factor-A.
Carcinoma, Squamous Cell
The ubiquitin-associated (UBA) domain of SCCRO/DCUN1D1 protein serves as a feedback regulator of biochemical and oncogenic activity.
Colorectal Neoplasms
MicroRNA-520b Functions as a Tumor Suppressor in Colorectal Cancer by Inhibiting DCUN1D1.
Frontotemporal Lobar Degeneration
DCUN1D1 is a risk factor for frontotemporal lobar degeneration.
Lung Neoplasms
DCUN1D1 facilitates tumor metastasis by activating FAK signaling and up-regulates PD-L1 in non-small-cell lung cancer.
Lung Neoplasms
Evidence for frequent concurrent DCUN1D1, FGFR1, BCL9 gene copy number amplification in squamous cell lung cancer.
Lymphatic Metastasis
DCUN1D1 facilitates tumor metastasis by activating FAK signaling and up-regulates PD-L1 in non-small-cell lung cancer.
Neoplasm Metastasis
DCUN1D1 facilitates tumor metastasis by activating FAK signaling and up-regulates PD-L1 in non-small-cell lung cancer.
Neoplasm Metastasis
Immunohistochemical Expression of DCUN1D1 in Non-small Cell Lung Carcinoma: Its Relation to Brain Metastasis.
Neoplasm Metastasis
MicroRNA-302 inhibits cell migration and invasion in cervical cancer by targeting DCUN1D1.
Neoplasm Metastasis
SCCRO (DCUN1D1) induces extracellular matrix invasion by activating matrix metalloproteinase 2.
Neoplasm Metastasis
The role of novel oncogenes squamous cell carcinoma-related oncogene and phosphatidylinositol 3-kinase p110alpha in squamous cell carcinoma of the oral tongue.
Neoplasms
Association of ring box-1 protein overexpression with clinicopathologic prognostic parameters in prostate carcinoma.
Neoplasms
Clinical significance of SCCRO (DCUN1D1) in prostate cancer and its proliferation-inhibiting effect on Lncap cells.
Neoplasms
Conjugation of the ubiquitin-like protein NEDD8 to cullin-2 is linked to von Hippel-Lindau tumor suppressor function.
Neoplasms
DCUN1D1 facilitates tumor metastasis by activating FAK signaling and up-regulates PD-L1 in non-small-cell lung cancer.
Neoplasms
DCUN1D1 promotes tumour progress in prostate cancer and its effect on DU145 in vitro.
Neoplasms
Evidence for frequent concurrent DCUN1D1, FGFR1, BCL9 gene copy number amplification in squamous cell lung cancer.
Neoplasms
Expression of DCUN1D1 in laryngeal squamous cell carcinoma and its inhibiting effect on TU-177 cells after interfered by RNA.
Neoplasms
Expression of Ring Box-1 protein and its relationship with Fuhrman grade and other clinical-pathological parameters in renal cell cancer.
Neoplasms
Immunohistochemical Expression of DCUN1D1 in Non-small Cell Lung Carcinoma: Its Relation to Brain Metastasis.
Neoplasms
MicroRNA-195 inhibits growth and invasion of laryngeal carcinoma cells by directly targeting DCUN1D1.
Neoplasms
MicroRNA-520b Functions as a Tumor Suppressor in Colorectal Cancer by Inhibiting DCUN1D1.
Neoplasms
Ran-mediated nuclear export of the von Hippel-Lindau tumor suppressor protein occurs independently of its assembly with cullin-2.
Neoplasms
SCCRO (DCUN1D1) induces extracellular matrix invasion by activating matrix metalloproteinase 2.
Neoplasms
SCCRO expression correlates with invasive progression in bronchioloalveolar carcinoma.
Neoplasms
SCCRO3 (DCUN1D3) antagonizes the neddylation and oncogenic activity of SCCRO (DCUN1D1).
Neoplasms
Squamous cell carcinoma related oncogene regulates angiogenesis through vascular endothelial growth factor-A.
Neoplasms
Squamous cell carcinoma related oncogene/DCUN1D1 is highly conserved and activated by amplification in squamous cell carcinomas.
Neoplasms
Squamous cell carcinoma-related oncogene is highly expressed in developing, normal, and adenomatous adrenal tissue but not in aggressive adrenocortical carcinomas.
Neoplasms
The relation between Ring Box-1 protein overexpression and tumor grade and stage in bladder urothelial cell carcinoma.
Neoplasms
The role of novel oncogenes squamous cell carcinoma-related oncogene and phosphatidylinositol 3-kinase p110alpha in squamous cell carcinoma of the oral tongue.
Neoplasms
The ubiquitin-associated (UBA) domain of SCCRO/DCUN1D1 protein serves as a feedback regulator of biochemical and oncogenic activity.
Neoplasms
The von Hippel-Lindau tumor suppressor gene product promotes, but is not essential for, NEDD8 conjugation to cullin-2.
Papilloma
MicroRNA?195 inhibits cell proliferation, migration and invasion by targeting defective in cullin neddylation 1 domain containing 1 in cervical cancer.
Prostatic Intraepithelial Neoplasia
Association of ring box-1 protein overexpression with clinicopathologic prognostic parameters in prostate carcinoma.
Prostatic Neoplasms
Clinical significance of SCCRO (DCUN1D1) in prostate cancer and its proliferation-inhibiting effect on Lncap cells.
Prostatic Neoplasms
DCUN1D1 promotes tumour progress in prostate cancer and its effect on DU145 in vitro.
Squamous Cell Carcinoma of Head and Neck
Expression of DCUN1D1 in laryngeal squamous cell carcinoma and its inhibiting effect on TU-177 cells after interfered by RNA.
Squamous Cell Carcinoma of Head and Neck
The role of novel oncogenes squamous cell carcinoma-related oncogene and phosphatidylinositol 3-kinase p110alpha in squamous cell carcinoma of the oral tongue.
Squamous Cell Carcinoma of Head and Neck
The ubiquitin-associated (UBA) domain of SCCRO/DCUN1D1 protein serves as a feedback regulator of biochemical and oncogenic activity.
Uterine Cervical Neoplasms
MicroRNA-218 inhibits EMT, migration and invasion by targeting SFMBT1 and DCUN1D1 in cervical cancer.
Uterine Cervical Neoplasms
MicroRNA-302 inhibits cell migration and invasion in cervical cancer by targeting DCUN1D1.
Uterine Cervical Neoplasms
MicroRNA?195 inhibits cell proliferation, migration and invasion by targeting defective in cullin neddylation 1 domain containing 1 in cervical cancer.
von Hippel-Lindau Disease
The SOCS box of SOCS-1 accelerates ubiquitin-dependent proteolysis of TEL-JAK2.
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ORGANISM
COMMENTARY
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
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brenda
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SOURCE TISSUE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
SOURCE
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LOCALIZATION
ORGANISM
UNIPROT
COMMENTARY
GeneOntology No.
LITERATURE
SOURCE
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GENERAL INFORMATION
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
malfunction
-
down-regulation of RBX1 significantly induces RhoB accumulation and blocks tumor suppressor RhoB degradation in the presence of cycloheximide
metabolism
physiological function
metabolism
-
in the nucleus, SCCRO enhances recruitment of Ubc12 to cullin 1 to promote neddylation. The enzyme facilitates the subcellular localization of neddylation components, which is required for cullin neddylation in vivo
metabolism
-
the enzyme functions as an E3 for related-to-ubiquitin protein modification of cullin 1
metabolism
-
the enzyme is an important component of the neddylation E3 complex that functions to recruit charged E2 and is involved in the release of inhibitory effects of CAND1 on cullin-RING ligase E3 complex assembly and activity. The enzyme binds to the components of the neddylation pathway (cullin-ROC1, Ubc12, and CAND1) and augments but is not required for cullin neddylation
metabolism
-
the function of RBX1 is to bind the ubiquitin-conjugating enzyme E2 and bring it into close proximity with the E3 substrate
metabolism
-
the Rbx1 subunit of SCF and VHL E3 ubiquitin ligase activates Rub1 modification of cullins Cdc53 and Cul2
physiological function
-
overexpression of RBX1 increases protein RUB modification of cullin-1. This effect is associated with reduced auxin response and severe growth defects
physiological function
-
the enzyme enhances cell proliferation by promoting cullin neddylation
physiological function
DCNL5 assists Cullin-bound RING-finger protein in neddylation and may be involved in innate immunity. DCNL5 is a direct substrate of the kinase IKKalpha during immune signalling. Upon activation of Toll-like receptors, DCNL5 gets rapidly and transiently phosphorylated on N-terminal serine residue S41. The phosphorylation is specifically mediated by IKKalpha and not IKKbeta
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UNIPROT
ENTRY NAME
ORGANISM
NO. OF AA
NO. OF TRANSM. HELICES
MOLECULAR WEIGHT[Da]
SOURCE
SEQUENCE
LOCALIZATION PREDICTION
The reliability class of the localization prediction ranges from 1 (very reliable) to 5 (not reliable).
The reliability class of the localization prediction ranges from 1 (very reliable) to 5 (not reliable). RBX1_HUMAN
108
0
12274
Swiss-Prot
other Location (Reliability: 3)
RBX1_MOUSE
108
0
12274
Swiss-Prot
other Location (Reliability: 3)
UBE2F_HUMAN
185
0
21077
Swiss-Prot
other Location (Reliability: 5)
UBE2F_RAT
185
0
21080
Swiss-Prot
Mitochondrion (Reliability: 5)
UBE2F_XENLA
185
0
21397
Swiss-Prot
other Location (Reliability: 5)
UBE2F_XENTR
185
0
21313
Swiss-Prot
other Location (Reliability: 5)
UBE2F_BOVIN
185
0
21133
Swiss-Prot
Mitochondrion (Reliability: 5)
UBE2F_CHICK
185
0
21229
Swiss-Prot
Mitochondrion (Reliability: 5)
UBE2F_DANRE
185
0
21019
Swiss-Prot
Mitochondrion (Reliability: 5)
A0A8J8WKF8_9EURO
118
0
13498
TrEMBL
other Location (Reliability: 1)
A0A7R8CHP0_LEPSM
123
0
13461
TrEMBL
other Location (Reliability: 2)
C0HBQ9_SALSA
185
0
21040
TrEMBL
other Location (Reliability: 4)
DCN1_YEAST
Saccharomyces cerevisiae (strain ATCC 204508 / S288c)
269
0
32204
Swiss-Prot
-
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PDB
SCOP
CATH
UNIPROT
ORGANISM
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SUBUNIT
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
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POSTTRANSLATIONAL MODIFICATION
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
phosphoprotein
DCNL5 is a direct substrate of the kinase IKKalpha during immune signalling. Upon activation of Toll-like receptors, DCNL5 gets rapidly and transiently phosphorylated on N-terminal serine residue S41
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CRYSTALLIZATION (Commentary)
ORGANISM
UNIPROT
LITERATURE
hanging drop vapor diffusion method, using 2% (w/v) PEG3350, 0.1M HEPES, 0.2 M L-Pro, pH 8.0
-
hanging drop vapor diffusion method, using about 20% (w/v) PEG3350, 0.2 M ammonium citrate, pH 7.0
-
structures of the neddylated and deneddylated COP9 signalosome-cullin-2 complexes. The structures suggest a conserved mechanism of COP9 signalosome activation, consisting of conformational clamping of the cullin-2 substrate by COP9 signalosome subunits CSN2/CSN4, release of the catalytic CSN5/CSN6 heterodimer and finally activation of the CSN5 deneddylation machinery. Cullin-2 activates CSN5/CSN6 in a neddylation-independent manner
hanging drop vapor diffusion method, using 400 mM ammonium acetate, 30% (w/v) PEG4000, and 0.1 M trisodium citrate (pH 5.6) at 20°C
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PROTEIN VARIANTS
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
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PURIFICATION (Commentary)
ORGANISM
UNIPROT
LITERATURE
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CLONED (Commentary)
ORGANISM
UNIPROT
LITERATURE
expressed in Escherichia coli or insect cells
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APPLICATION
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
analysis
development of peptides to probe the protein-protein interaction between the cullin-2 scaffold protein and the adaptor subunit elongin BC within the context of the von Hippel-Lindau complex. Peptides MSLKPRVV and MS-cyclohexylglycine-KPRVV can disrupt the native interaction between the von Hippel-Landau complex and Cul2
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REF.
AUTHORS
TITLE
JOURNAL
VOL.
PAGES
YEAR
ORGANISM (UNIPROT)
PUBMED ID
SOURCE
Onel, M.; Sumbul, F.; Liu, J.; Nussinov, R.; Haliloglu, T.
Cullin neddylation may allosterically tune polyubiquitin chain length and topology
Biochem. J.
474
781-795
2017
Homo sapiens (P62877)
brenda
Duda, D.; Borg, L.; Scott, D.; Hunt, H.; Hammel, M.; Schulman, B.
Structural insights into NEDD8 activation of Cullin-RING ligases conformational control of conjugation
Cell
134
995-1006
2008
Homo sapiens
brenda
Scott, D.; Sviderskiy, V.; Monda, J.; Lydeard, J.; Cho, S.; Harper, J.; Schulman, B.
Structure of a RING E3 trapped in action reveals ligation mechanism for the ubiquitin-like protein NEDD8
Cell
157
1671-1684
2014
Homo sapiens
brenda
Dharmasiri, S.; Dharmasiri, N.; Hellmann, H.; Estelle, M.
The RUB/Nedd8 conjugation pathway is required for early development in Arabidopsis
EMBO J.
22
1762-1770
2003
Arabidopsis thaliana
brenda
Bagchi, R.; Melnyk, C.; Christ, G.; Winkler, M.; Kirchsteiner, K.; Salehin, M.; Mergner, J.; Niemeyer, M.; Schwechheimer, C.; Caldern Villalobos, L.; Estelle, M.
The Arabidopsis ALF4 protein is a regulator of SCF E3 ligases
EMBO J.
37
255-268
2018
Arabidopsis thaliana
brenda
Megumi, Y.; Miyauchi, Y.; Sakurai, H.; Nobeyama, H.; Lorick, K.; Nakamura, E.; Chiba, T.; Tanaka, K.; Weissman, A.; Kirisako, T.; Ogawa, O.; Iwai, K.
Multiple roles of Rbx1 in the VBC-Cul2 ubiquitin ligase complex
Genes Cells
10
679-691
2005
Homo sapiens
brenda
Kamura, T.; Conrad, M.; Yan, Q.; Conaway, R.; Conaway, J.
The Rbx1 subunit of SCF and VHL E3 ubiquitin ligase activates Rub1 modification of cullins Cdc53 and Cul2
Genes Dev.
13
2928-2933
1999
Homo sapiens
brenda
Kim, A.; Bommelje, C.; Lee, B.; Yonekawa, Y.; Choi, L.; Morris, L.; Huang, G.; Kaufman, A.; Ryan, R.; Hao, B.; Ramanathan, Y.; Singh, B.
SCCRO (DCUN1D1) is an essential component of the E3 complex for neddylation
J. Biol. Chem.
283
33211-33220
2008
Mus musculus
-
brenda
Huang, G.; Kaufman, A.; Ramanathan, Y.; Singh, B.
SCCRO (DCUN1D1) promotes nuclear translocation and assembly of the neddylation E3 complex
J. Biol. Chem.
286
10297-10304
2011
Homo sapiens
brenda
Kurz, T.; Chou, Y.; Willems, A.; Meyer-Schaller, N.; Hecht, M.; Tyers, M.; Peter, M.; Sicheri, F.
Dcn1 functions as a scaffold-type E3 ligase for cullin neddylation
Mol. Cell.
29
23-35
2008
Saccharomyces cerevisiae (Q12395)
brenda
Huang, D.; Ayrault, O.; Hunt, H.; Taherbhoy, A.; Duda, D.; Scott, D.; Borg, L.; Neale, G.; Murray, P.; Roussel, M.; Schulman, B.
E2-RING expansion of the NEDD8 cascade confers specificity to cullin modification
Mol. Cell.
33
483-495
2009
Homo sapiens
brenda
Scott, D.; Monda, J.; Grace, C.; Duda, D.; Kriwacki, R.; Kurz, T.; Schulman, B.
A dual E3 mechanism for Rub1 ligation to Cdc53
Mol. Cell.
39
784-796
2010
Saccharomyces cerevisiae
brenda
Xu, J.; Li, L.; Yu, G.; Ying, W.; Gao, Q.; Zhang, W.; Li, X.; Ding, C.; Jiang, Y.; Wei, D.; Duan, S.; Lei, Q.; Li, P.; Shi, T.; Qian, X.; Qin, J.; Jia, L.
The neddylation-cullin 2-RBX1 E3 ligase axis targets tumor suppressor RhoB for degradation in liver cancer
Mol. Cell. Proteomics
14
499-509
2015
Homo sapiens
brenda
Sakata, E.; Yamaguchi, Y.; Miyauchi, Y.; Iwai, K.; Chiba, T.; Saeki, Y.; Matsuda, N.; Tanaka, K.; Kato, K.
Direct interactions between NEDD8 and ubiquitin E2 conjugating enzymes upregulate cullin-based E3 ligase activity
Nat. Struct. Mol. Biol.
14
167-168
2007
Homo sapiens
brenda
Rahighi, S.; Dikic, I.
Conformational flexibility and rotation of the RING domain in activation of cullin-RING ligases
Nat. Struct. Mol. Biol.
18
863-865
2011
Homo sapiens
-
brenda
Calabrese, M.; Scott, D.; Duda, D.; Grace, C.; Kurinov, I.; Kriwacki, R.; Schulman, B.
A RING E3-substrate complex poised for ubiquitin-like protein transfer Structural insights into cullin-RING ligases
Nat. Struct. Mol. Biol.
18
947-949
2011
Homo sapiens
brenda
Kurz, T.; zl, N.; Rudolf, F.; ORourke, S.; Luke, B.; Hofmann, K.; Hyman, A.; Bowerman, B.; Peter, M.
The conserved protein DCN-1/Dcn1p is required for cullin neddylation in C. elegans and S. cerevisiae
Nature
435
1257-1261
2005
Saccharomyces cerevisiae, Caenorhabditis elegans
brenda
Gray, W.; Hellmann, H.; Dharmasiri, S.; Estelle, M.
Role of the Arabidopsis RING-H2 protein RBX1 in RUB modification and SCF function
Plant Cell
14
2137-2144
2002
Arabidopsis thaliana
brenda
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
brenda
Cardote, T.A.F.; Ciulli, A.
Structure-guided design of peptides as tools to probe the protein-protein interaction between cullin-2 and elongin BC substrate adaptor in cullin RING E3 ubiquitin ligases
ChemMedChem
12
1491-1496
2017
Homo sapiens (Q13617)
brenda
Coleman, K.E.; Bekes, M.; Chapman, J.R.; Crist, S.B.; Jones, M.J.; Ueberheide, B.M.; Huang, T.T.
SENP8 limits aberrant neddylation of NEDD8 pathway components to promote cullin-RING ubiquitin ligase function
eLife
6
e24325
2017
Homo sapiens (P62877)
brenda
Faull, S.V.; Lau, A.M.C.; Martens, C.; Ahdash, Z.; Hansen, K.; Yebenes, H.; Schmidt, C.; Beuron, F.; Cronin, N.B.; Morris, E.P.; Politis, A.
Structural basis of Cullin 2 RING E3 ligase regulation by the COP9 signalosome
Nat. Commun.
10
3814
2019
Homo sapiens (Q13617)
brenda
Baek, K.; Krist, D.T.; Prabu, J.R.; Hill, S.; Kluegel, M.; Neumaier, L.M.; von Gronau, S.; Kleiger, G.; Schulman, B.A.
NEDD8 nucleates a multivalent cullin-RING-UBE2D ubiquitin ligation assembly
Nature
578
461-466
2020
Homo sapiens (P62877)
brenda
Thomas, Y.; Scott, D.C.; Kristariyanto, Y.A.; Rinehart, J.; Clark, K.; Cohen, P.; Kurz, T.
The NEDD8 E3 ligase DCNL5 is phosphorylated by IKK alpha during Toll-like receptor activation
PLoS ONE
13
e0199197
2018
Homo sapiens (Q9BTE7)
brenda
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