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Information on EC 2.3.2.32 - cullin-RING-type E3 NEDD8 transferase
for references in articles please use BRENDA:EC2.3.2.32
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EC Tree 2 Transferases
2.3 Acyltransferases
2.3.2 Aminoacyltransferases
2.3.2.32 cullin-RING-type E3 NEDD8 transferase
IUBMB 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.
The enzyme appears in viruses and cellular organisms
- 2.3.2.32
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cullins
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neddylation
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elongins
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carcinoma-related
- hippel-lindau
- analysis
Reaction Schemes
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[E2 NEDD8-conjugating enzyme]-S-[NEDD8-protein]-yl-L-cysteine
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[cullin]-L-lysine
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[E2 NEDD8-conjugating enzyme]-L-cysteine
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[cullin]-N6-[NEDD8-protein]-yl-L-lysine
Synonyms
sccro, dcun1d1, cullin-2, rbx-1, dcn-1, dcun1d5, dcn1p, dcnl5, nedd8 e3 ligase, cullin 2-rbx1 e3 ligase, more
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SYNONYM 
ORGANISM
UNIPROT
COMMENTARY 
LITERATURE
CRL2
the enzyme complex is composed of the CUL2 scaffold, the RING-domain protein RBX1, the adapter comprising ELOB and ELOC proteins, and a substrate receptor protein containing a BC-box motif that binds the adapter
CRL5
the multi-protein complex and consists of a scaffold protein cullin 5, a RING protein RBX2, adaptor proteins elongin B/C, and a substrate receptor protein SOCS
cullin 2-RBX1 E3 ligase
cullin-2
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
MetaCyc
protein NEDDylation
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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
LITERATURE
COMMENTARY
Reversibility
r=reversible
ir=irreversible
?=not specified
r=reversible
ir=irreversible
?=not specified
Rheb + ?
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Substrates: Rheb is polyubiquitinated at K109, K135, K151, and K178
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[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
[E2 NEDD8-conjugating enzyme]-S-[NEDD8-protein UBE2F]-yl-L-cysteine + [cullin 5]-L-lysine
[E2 NEDD8-conjugating enzyme]-L-cysteine + [cullin 5]-N6-[NEDD8-protein UBE2F]-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 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 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
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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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[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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[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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Substrates: 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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Substrates: 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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Substrates: the NEDD8 conjugating enzyme UBE2M binds specifically to RBX1
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additional information
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Substrates: 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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Substrates: 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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Substrates: KLHL9 acts as a specific adaptor protein for the CUL3-RBX1 ligase complex to interact with and ubiquitinate Rheb
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additional information
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Substrates: KLHL9 acts as a specific adaptor protein for the CUL3-RBX1 ligase complex to interact with and ubiquitinate Rheb
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additional information
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Substrates: KLHL9 acts as a specific adaptor protein for the CUL3-RBX1 ligase complex to interact with and ubiquitinate Rheb
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additional information
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Substrates: 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
LITERATURE
COMMENTARY
REVERSIBILITY
r=reversible
ir=irreversible
?=not specified
r=reversible
ir=irreversible
?=not specified
[E2 NEDD8-conjugating enzyme]-S-[NEDD8-protein UBE2F]-yl-L-cysteine + [cullin 5]-L-lysine
[E2 NEDD8-conjugating enzyme]-L-cysteine + [cullin 5]-N6-[NEDD8-protein UBE2F]-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
additional information
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Substrates: 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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[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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[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
Substrates: -
Products: -
Products: -
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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
Substrates: -
Products: -
Products: -
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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
-
Substrates: -
Products: -
Products: -
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INHIBITOR
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
2-[5-[(2-[[(4-chlorophenyl)methyl]sulfanyl]-5-methyl[1,2,4]triazolo[1,5-a]pyrimidin-7-yl)sulfanyl]-1H-tetrazol-1-yl]-N,N-dimethylethan-1-amine
WS-383
3-methyl-N-[(5S)-3-methyl-1-phenyl-4,5,6,7-tetrahydro-1H-pyrazolo[3,4-b]pyridin-5-yl]benzamide
-
4-(4-methylphenyl)-2-[(prop-2-yn-1-yl)sulfanyl]-6-[(1,3-thiazol-2-yl)sulfanyl]pyrimidine-5-carbonitrile
DC-2
4-[(1-methyl-1H-tetrazol-5-yl)sulfanyl]-6-(2-oxo-2H-1-benzopyran-6-yl)-2-[(prop-2-yn-1-yl)sulfanyl]pyrimidine-5-carbonitrile
DC-1
7-[(1-methyl-1H-tetrazol-5-yl)sulfanyl]-5-phenyl[1,2,4]triazolo[1,5-a]pyrimidine
-
CAND1
binds unneddylated cullin 2 and inhibits the degradation of CRL2 substrates dependent on CRL2 substrate affinity; binds unneddylated cullin 2 and inhibits the degradation of CRL2 substrates dependent on CRL2 substrate affinity; binds unneddylated cullin 2 and inhibits the degradation of CRL2 substrates dependent on CRL2 substrate affinity; binds unneddylated cullin 2 and inhibits the degradation of CRL2 substrates dependent on CRL2 substrate affinity
-
N,N-dimethyl-2-[5-[(5-phenyl[1,2,4]triazolo[1,5-a]pyrimidin-7-yl)sulfanyl]-1H-tetrazol-1-yl]ethan-1-amine
-
N-(1-benzylpiperidin-4-yl)-N'-[3-(trifluoromethyl)phenyl]urea
potent inhibitor
N-acetyl-3-(6-chloro-1,3-benzothiazol-2-yl)-L-alanyl-L-isoleucyl-L-lysyl-L-leucinamide
-
N-acetyl-3-(naphthalen-2-yl)-L-alanyl-L-isoleucyl-L-lysyl-L-leucinamide
the compound blocks the interactions of the enzyme with its binding partners UBC12 and UBC2E
N-acetyl-3-[6-(propan-2-yl)-1,3-benzothiazol-2-yl]-L-alanyl-L-isoleucinamide
-
N-acetyl-3-[6-(propan-2-yl)-1,3-benzothiazol-2-yl]-L-alanyl-L-isoleucyl-L-lysinamide
-
N-acetyl-3-[6-(propan-2-yl)-1,3-benzothiazol-2-yl]-L-alanyl-L-isoleucyl-L-lysyl-L-leucinamide
-
N-acetyl-L-methionyl-L-isoleucyl-L-lysyl-L-leucinamide
the compound blocks the interactions of the enzyme with its binding partners UBC12 and UBC2E
N-acetyl-L-methionyl-L-isoleucyl-L-lysyl-L-leucyl-L-phenylalanyl-L-seryl-L-leucyl-L-lysyl-L-glutaminyl-L-glutaminyl-L-lysyl-L-lysinamide
the compound blocks the interactions of the enzyme with its binding partners UBC12 and UBC2E
N-benzyl-N-(1-butylpiperidin-4-yl)-N'-(3,4-dichlorophenyl)urea
potent inhibitor
N-benzyl-N-[1-(pentan-2-yl)piperidin-4-yl]-N'-[3-(trifluoromethyl)phenyl]urea
potent inhibitor
N-propanoyl-3-(naphthalen-2-yl)-L-alany-L-isoleucyl-L-lysyl-L-leucinamide
the compound blocks the interactions of the enzyme with its binding partners UBC12 and UBC2E
N-propanoyl-3-(naphthalen-2-yl)-L-alanyl-L-isoleucyl-N-(diphenylmethyl)-L-lysinamide
the compound blocks the interactions of the enzyme with its binding partners UBC12 and UBC2E
N-[(1S)-1-cyclohexyl-2-[3-(morpholin-4-yl)propanamido]ethyl]-N2-propanoyl-3-[6-(propan-2-yl)-1,3-benzothiazol-2-yl]-L-alaninamide
DI-591
N-[(1S)-2-amino-1-cyclohexylethyl]-N2-propanoyl-3-[6-(propan-2-yl)-1,3-benzothiazol-2-yl]-L-alaninamide
-
N-[(2H-1,3-benzodioxol-5-yl)methyl]-N-(1-propylpiperidin-4-yl)-N'-[3-(trifluoromethyl)phenyl]urea
potent inhibitor
N-[(4S,5S)-7-ethyl-4-(4-fluorophenyl)-3-methyl-1-phenyl-4,5,6,7-tetrahydro-1H-pyrazolo[3,4-b]pyridin-5-yl]-3-methylbenzamide
-
N-[2-[([1-(pentan-2-yl)piperidin-4-yl][[3-(trifluoromethyl)phenyl]carbamoyl]amino)methyl]phenyl]prop-2-enamide
potent inhibitor
N2-acetyl-N-[(2S,3S)-1-amino-3-methylpentan-2-yl]-3-[6-(propan-2-yl)-1,3-benzothiazol-2-yl]-L-alaninamide
-
N2-[(2S)-2-cyclopentyl-2-[(N-propanoyl-3-(naphthalen-2-yl)-L-alanyl)amino]acetyl]-N-(diphenylmethyl)-L-lysinamide
the compound blocks the interactions of the enzyme with its binding partners UBC12 and UBC2E
N2-[(2S)-2-[[3-(6-chloro-1,3-benzothiazol-2-yl)-N-propanoyl-L-alanyl]amino]-2-(oxan-4-yl)acetyl]-N-[(4R)-3,4-dihydro-2H-1-benzopyran-4-yl]-L-lysinamide
DI-404
N2-[(2S)-2-[[3-(6-chloro-1,3-benzothiazol-2-yl)-N-propanoyl-L-alanyl]amino]-2-cyclopentylacetyl]-N-(diphenylmethyl)-L-lysinamide
the compound blocks the interactions of the enzyme with its binding partners UBC12 and UBC2E
N2-[(2S)-2-[[3-(6-chloro-1,3-benzothiazol-2-yl)-N-propanoyl-L-alanyl]amino]-2-cyclopentylacetyl]-N-[(4R)-3,4-dihydro-2H-1-benzopyran-4-yl]-L-lysinamide
the compound blocks the interactions of the enzyme with its binding partners UBC12 and UBC2E
N2-[(2S)-2-[[3-(6-chloro-1,3-benzothiazol-2-yl)-N-propanoyl-L-alanyl]amino]-2-cyclopentylacetyl]-N-[(4R)-3,4-dihydro-2H-1-benzopyran-4-yl]-N6,N6-dimethyl-L-lysinamide
the compound blocks the interactions of the enzyme with its binding partners UBC12 and UBC2E
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ACTIVATING COMPOUND
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
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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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Ki VALUE [mM]
INHIBITOR
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
0.000034
N-acetyl-3-(6-chloro-1,3-benzothiazol-2-yl)-L-alanyl-L-isoleucyl-L-lysyl-L-leucinamide
pH and temperature not specified in the publication
0.0036
N-acetyl-3-(naphthalen-2-yl)-L-alanyl-L-isoleucyl-L-lysyl-L-leucinamide
pH and temperature not specified in the publication
0.000292
N-acetyl-3-[6-(propan-2-yl)-1,3-benzothiazol-2-yl]-L-alanyl-L-isoleucinamide
pH and temperature not specified in the publication
0.000174
N-acetyl-3-[6-(propan-2-yl)-1,3-benzothiazol-2-yl]-L-alanyl-L-isoleucyl-L-lysinamide
pH and temperature not specified in the publication
0.0000047
N-acetyl-3-[6-(propan-2-yl)-1,3-benzothiazol-2-yl]-L-alanyl-L-isoleucyl-L-lysyl-L-leucinamide
pH and temperature not specified in the publication
0.13
N-acetyl-L-methionyl-L-isoleucyl-L-lysyl-L-leucinamide
pH and temperature not specified in the publication
0.0051
N-acetyl-L-methionyl-L-isoleucyl-L-lysyl-L-leucyl-L-phenylalanyl-L-seryl-L-leucyl-L-lysyl-L-glutaminyl-L-glutaminyl-L-lysyl-L-lysinamide
pH and temperature not specified in the publication
0.0011
N-propanoyl-3-(naphthalen-2-yl)-L-alany-L-isoleucyl-L-lysyl-L-leucinamide
pH and temperature not specified in the publication
0.000097
N-propanoyl-3-(naphthalen-2-yl)-L-alanyl-L-isoleucyl-N-(diphenylmethyl)-L-lysinamide
pH and temperature not specified in the publication
0.000012
N-[(1S)-1-cyclohexyl-2-[3-(morpholin-4-yl)propanamido]ethyl]-N2-propanoyl-3-[6-(propan-2-yl)-1,3-benzothiazol-2-yl]-L-alaninamide
pH and temperature not specified in the publication
0.000013
N-[(1S)-2-amino-1-cyclohexylethyl]-N2-propanoyl-3-[6-(propan-2-yl)-1,3-benzothiazol-2-yl]-L-alaninamide
pH and temperature not specified in the publication
0.000019 - 0.000066
N2-acetyl-N-[(2S,3S)-1-amino-3-methylpentan-2-yl]-3-[6-(propan-2-yl)-1,3-benzothiazol-2-yl]-L-alaninamide
0.000036
N2-[(2S)-2-cyclopentyl-2-[(N-propanoyl-3-(naphthalen-2-yl)-L-alanyl)amino]acetyl]-N-(diphenylmethyl)-L-lysinamide
pH and temperature not specified in the publication
0.000019
N2-acetyl-N-[(2S,3S)-1-amino-3-methylpentan-2-yl]-3-[6-(propan-2-yl)-1,3-benzothiazol-2-yl]-L-alaninamide
pH and temperature not specified in the publication
0.000066
N2-acetyl-N-[(2S,3S)-1-amino-3-methylpentan-2-yl]-3-[6-(propan-2-yl)-1,3-benzothiazol-2-yl]-L-alaninamide
pH and temperature not specified in the publication
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IC50 VALUE [mM]
INHIBITOR
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
0.000011
2-[5-[(2-[[(4-chlorophenyl)methyl]sulfanyl]-5-methyl[1,2,4]triazolo[1,5-a]pyrimidin-7-yl)sulfanyl]-1H-tetrazol-1-yl]-N,N-dimethylethan-1-amine
Homo sapiens
pH and temperature not specified in the publication
0.0002
4-(4-methylphenyl)-2-[(prop-2-yn-1-yl)sulfanyl]-6-[(1,3-thiazol-2-yl)sulfanyl]pyrimidine-5-carbonitrile
Homo sapiens
pH and temperature not specified in the publication
0.0051
4-[(1-methyl-1H-tetrazol-5-yl)sulfanyl]-6-(2-oxo-2H-1-benzopyran-6-yl)-2-[(prop-2-yn-1-yl)sulfanyl]pyrimidine-5-carbonitrile
Homo sapiens
pH and temperature not specified in the publication
0.00582
7-[(1-methyl-1H-tetrazol-5-yl)sulfanyl]-5-phenyl[1,2,4]triazolo[1,5-a]pyrimidine
Homo sapiens
pH and temperature not specified in the publication
0.00013
N,N-dimethyl-2-[5-[(5-phenyl[1,2,4]triazolo[1,5-a]pyrimidin-7-yl)sulfanyl]-1H-tetrazol-1-yl]ethan-1-amine
Homo sapiens
pH and temperature not specified in the publication
0.008
N-(1-benzylpiperidin-4-yl)-N'-[3-(trifluoromethyl)phenyl]urea
Homo sapiens
pH and temperature not specified in the publication
0.00006
N-benzyl-N-[1-(pentan-2-yl)piperidin-4-yl]-N'-[3-(trifluoromethyl)phenyl]urea
Homo sapiens
pH and temperature not specified in the publication
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ORGANISM
COMMENTARY
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
-
-
-
brenda
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SOURCE TISSUE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
SOURCE
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LOCALIZATION
ORGANISM
UNIPROT
COMMENTARY
GeneOntology No.
LITERATURE
SOURCE
Highest Expressing Human Cell Lines
Cell Line LinksPlease wait a moment until the data is sorted. This message will disappear when the data is sorted.
GENERAL INFORMATION
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
malfunction
metabolism
physiological function
malfunction
-
down-regulation of RBX1 significantly induces RhoB accumulation and blocks tumor suppressor RhoB degradation in the presence of cycloheximide
malfunction
enzyme-deficient mice develop an early-onset fatal inflammatory disorder, characterized by disrupted regulatory T cell homeostasis and suppressive functions
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 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 enzyme functions as an E3 for related-to-ubiquitin protein modification of cullin 1
metabolism
-
the Rbx1 subunit of SCF and VHL E3 ubiquitin ligase activates Rub1 modification of cullins Cdc53 and Cul2
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 CUL3-RBX1-KLHL9 complex functions as a mTORC1 activator by acting as an E3 ubiquitin ligase for Rheb and supports amino acid-induced mTORC1 activation
metabolism
DCAF1 is an essential substrate receptor for the cullin 4 RING ubiquitin E3 ligase family. DCAF1 is implicated in fundamental cellular processes, ranging from DNA replication, cell cycle progression, transcription, to zygotic development and reproduction
metabolism
-
cullin-2 forms a functional E3 ligase complex with elongin B, elongin C, RING-box protein 1 (RBX1), as well as the substrate recognition subunit to promote the substrate ubiquitination and degradation. Cullin-2 N-terminus binds with elongin B, elongin C, and the substrate recognition subunit von Hippel-Lindau, while the C-terminus binds with RBX1. RBX1 then promotes the neddylation of cullin-2, which is essential for activating the CRL-mediated ubiquitin transfer from the ubiquitin-conjugating enzyme E2, and eventual ubiquitin chain formation on the substrate executed by E3
metabolism
RBX1/2 recruits ubiquitin-loaded E2 and catalyzes ubiquitin transferred from E2 to the substrate recognized by the receptor protein SOCS. Multiple rounds of this E1/E2/E3-mediated chain reaction lead to substrate polyubiquitination, and polyubiquitinated substrate is then recognized by the 26S proteasome for subsequent degradation
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
physiological function
the enzyme is essential for the maintenance of an effector regulatory T cell subpopulation, and regulates several inflammatory pathways. The Ube2m-enzyme axis is specifically required for intrinsic regulatory processes in regulatory T cells. The enzyme also plays Ube2m-independent roles in maintaining the fitness of regulatory T cells
physiological function
the enzyme controls cell cycle progression and cell proliferation through regulation of cyclin D1 protein stability. The enzyme regulates cyclin D1 ubiquitination and proteasome degradation in a phosphorylation-dependent manner
physiological function
-
the enzyme plays an important role in the development of the germline
physiological function
cullin 2 E3 ubiquitin ligase and ubiquitin-specific peptidase-2 coordinately regulate antithrombin ubiquitination and degradation. Cullin 2 is an E3 ubiquitin ligase that ubiquitinates antithrombin and promotes its proteasomal degradation
physiological function
the enzyme degrades a variety of substrates, which are involved in an array of biological processes, including cytokine signal transduction, inflammation, and oncogenesis. The enzyme is hijacked by a variety of viral proteins to degrade host anti-viral proteins, which facilitates virus infection
Show AA Sequence and Transmembrane Helices (1890 entries)
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Please use the AA Sequence and Transmembrane Helices Search for a specific query.
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PDB
SCOP
CATH
UNIPROT
ORGANISM
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MOLECULAR WEIGHT
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
1561000
multi-angle light scattering coupled with gel filtration
1582000
calculated from amino acid sequence
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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
additional information
additional information
an N-terminally truncated tetramerization-deficient enzyme mutant has higher ubiquitin ligase activity compared to the wild type
additional information
an N-terminally truncated tetramerization-deficient enzyme mutant has higher ubiquitin ligase activity compared to the wild type
additional information
an N-terminally truncated tetramerization-deficient enzyme mutant has higher ubiquitin ligase activity compared to the wild type
additional information
an N-terminally truncated tetramerization-deficient enzyme mutant has higher ubiquitin ligase activity compared to the wild type
additional information
an N-terminally truncated tetramerization-deficient enzyme mutant has higher ubiquitin ligase activity compared to the wild type
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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
medicine
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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
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
Caenorhabditis elegans, Saccharomyces cerevisiae
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
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
Homo sapiens
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
Liu, X.; Zurlo, G.; Zhang, Q.
The roles of cullin-2 E3 ubiquitin ligase complex in cancer
Adv. Exp. Med. Biol.
1217
173-186
2020
Caenorhabditis elegans
brenda
Zhou, H.; Lu, J.; Yang, C.Y.; Sun, Y.; Wang, S.
Targeting DCN1-UBC12 protein-protein interaction for regulation of neddylation pathway
Adv. Exp. Med. Biol.
1217
349-362
2020
Homo sapiens (Q96GG9)
brenda
Ares, G.R.
Ubiquitination of NKCC2 by the cullin-RING E3 ubiquitin ligase family in the thick ascending limb of the loop of Henle
Am. J. Physiol. Renal Physiol.
324
F315-F328
2023
Rattus norvegicus (A0A0G2K8N8)
brenda
Yao, Y.; Hong, S.; Yoshida, S.; Swaroop, V.; Curtin, B.; Inoki, K.
The Cullin3-Rbx1-KLHL9 E3 ubiquitin ligase complex ubiquitinates Rheb and supports amino acid-induced mTORC1 activation
Cell Rep.
44
115101
2025
Homo sapiens (Q13618), Homo sapiens (P62877), Homo sapiens (Q9P2J3)
brenda
Lu, K.; Zhang, M.; Wei, G.; Xiao, G.; Tong, L.; Chen, D.
Multiple cullin-associated E3 ligases regulate cyclin D1 protein stability
Elife
12
e80327
2023
Homo sapiens (Q14145), Homo sapiens (Q92466), Homo sapiens (Q9NYS7)
brenda
Mohamed, W.I.; Schenk, A.D.; Kempf, G.; Cavadini, S.; Basters, A.; Potenza, A.; Abdul Rahman, W.; Rabl, J.; Reichermeier, K.; Thomae, N.H.
The CRL4DCAF1 cullin-RING ubiquitin ligase is activated following a switch in oligomerization state
EMBO J.
40
e108008
2021
Homo sapiens (Q16531), Homo sapiens (P62877), Homo sapiens (Q13619), Homo sapiens (Q13620), Homo sapiens (Q9Y4B6)
brenda
Xu, D.; Wu, J.; Chen, J.; Jiang, L.; Chen, J.; Bao, W.; Chen, X.; Yang, Q.; Zhang, X.; Yao, L.; Su, H.; Liu, J.
Cullin 2-RBX1 E3 ligase and USP2 regulate antithrombin ubiquitination and stability
FASEB J.
35
e21800
2021
Homo sapiens (P62877), Homo sapiens (Q13617)
brenda
Mohanty, P.; Chatterjee, K.S.; Das, R.
NEDD8 deamidation inhibits cullin RING ligase dynamics
Front. Immunol.
12
695331
2021
Homo sapiens (P62877)
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 (P62878)
brenda
Horn-Ghetko, D.; Hopf, L.; Tripathi-Giesgen, I.; Du, J.; Kostrhon, S.; Vu, D.; Beier, V.; Steigenberger, B.; Prabu, J.; Stier, L.; Bruss, E.; Mann, M.; Xiong, Y.; Schulman, B.
Noncanonical assembly, neddylation and chimeric cullin-RING/RBR ubiquitylation by the 1.8 MDa CUL9 E3 ligase complex
Nat. Struct. Mol. Biol.
31
1083-1094
2024
Homo sapiens (P62877), Homo sapiens (Q8IWT3)
brenda
Wang, K.; Diaz, S.; Li, L.; Lohman, J.R.; Liu, X.
CAND1 inhibits cullin-2-RING ubiquitin ligases for enhanced substrate specificity
Nat. Struct. Mol. Biol.
31
323-335
2024
Homo sapiens (P62877), Homo sapiens (Q13617), Homo sapiens (Q15370), Homo sapiens (Q15369)
brenda
Zhao, Y.; Xiong, X.; Sun, Y.
Cullin-RING ligase 5 Functional characterization and its role in human cancers
Semin. Cancer Biol.
67
61-79
2020
Homo sapiens (Q93034), Homo sapiens (Q9UBF6)
brenda
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