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Information on EC 2.3.2.32 - cullin-RING-type E3 NEDD8 transferase

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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: Q9BTE7
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Word Map
The enzyme appears in viruses and cellular organisms
Reaction Schemes
[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
SYNONYM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
DCN1-like protein 5
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RBX1
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-
-
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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.
ORGANISM
COMMENTARY hide
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
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UniProt
Manually annotated by BRENDA team
GENERAL INFORMATION
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
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
UNIPROT
ENTRY NAME
ORGANISM
NO. OF AA
NO. OF TRANSM. HELICES
MOLECULAR WEIGHT[Da]
SOURCE
SEQUENCE
LOCALIZATION PREDICTION?
DCNL5_HUMAN
237
0
27508
Swiss-Prot
-
POSTTRANSLATIONAL MODIFICATION
ORGANISM
UNIPROT
COMMENTARY hide
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
REF.
AUTHORS
TITLE
JOURNAL
VOL.
PAGES
YEAR
ORGANISM (UNIPROT)
PUBMED ID
SOURCE
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)
Manually annotated by BRENDA team