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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.
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UNIPROT: Q13617
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Word Map
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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
[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, dcun1d5, dcn1p, dcnl5, nedd8 e3 ligase, cullin 2-rbx1 e3 ligase, more
SYNONYM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
RBX1
-
-
-
-
PATHWAY SOURCE
PATHWAYS
-
-
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.
ORGANISM
COMMENTARY hide
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
isoform cullin-2
UniProt
Manually annotated by BRENDA team
UNIPROT
ENTRY NAME
ORGANISM
NO. OF AA
NO. OF TRANSM. HELICES
MOLECULAR WEIGHT[Da]
SOURCE
SEQUENCE
LOCALIZATION PREDICTION?
CUL2_HUMAN
745
0
86983
Swiss-Prot
-
CRYSTALLIZATION (Commentary)
ORGANISM
UNIPROT
LITERATURE
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
APPLICATION
ORGANISM
UNIPROT
COMMENTARY hide
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
REF.
AUTHORS
TITLE
JOURNAL
VOL.
PAGES
YEAR
ORGANISM (UNIPROT)
PUBMED ID
SOURCE
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)
Manually annotated by BRENDA team
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)
Manually annotated by BRENDA team