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Information on EC 2.3.2.27 - RING-type E3 ubiquitin transferase and Organism(s) Mus musculus and UniProt Accession Q3U827

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EC Tree
     2 Transferases
         2.3 Acyltransferases
             2.3.2 Aminoacyltransferases
                2.3.2.27 RING-type E3 ubiquitin transferase
IUBMB Comments
RING E3 ubiquitin transferases serve as mediators bringing the ubiquitin-charged E2 ubiquitin-conjugating enzyme (EC 2.3.2.23) and an acceptor protein together to enable the direct transfer of ubiquitin through the formation of an isopeptide bond between the C-terminal glycine residue of ubiquitin and the epsilon-amino group of an L-lysine residue of the acceptor protein. Unlike EC 2.3.2.26, HECT-type E3 ubiquitin transferase, the RING-E3 domain does not form a catalytic thioester intermediate with ubiquitin. Many members of the RING-type E3 ubiquitin transferase family are not able to bind a substrate directly, and form a complex with a cullin scaffold protein and a substrate recognition module (the complexes are named CRL for Cullin-RING-Ligase). In these complexes, the RING-type E3 ubiquitin transferase provides an additional function, mediating the transfer of a NEDD8 protein from a dedicated E2 carrier to the cullin protein (see EC 2.3.2.32, cullin-RING-type E3 NEDD8 transferase). cf. EC 2.3.2.31, RBR-type E3 ubiquitin transferase.
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Mus musculus
UNIPROT: Q3U827
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The taxonomic range for the selected organisms is: Mus musculus
The enzyme appears in selected viruses and cellular organisms
Reaction Schemes
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[E2 ubiquitin-conjugating enzyme]-S-ubiquitinyl-L-cysteine
+
[acceptor protein]-L-lysine
=
[E2 ubiquitin-conjugating enzyme]-L-cysteine
+
[acceptor protein]-N6-ubiquitinyl-L-lysine
[E2 ubiquitin-conjugating enzyme]-S-ubiquitinyl-L-cysteine
+
[acceptor protein]-L-lysine
=
[E2 ubiquitin-conjugating enzyme]-L-cysteine
+
[acceptor protein]-N6-ubiquitinyl-L-lysine
Synonyms
brca1, parkin, e3 ubiquitin ligase, e3 ligase, c-cbl, ciap2, trim5alpha, rnf43, trim25, trim5, more
SYNONYM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
TRIM3
-
-
PATHWAY SOURCE
PATHWAYS
-
-
SYSTEMATIC NAME
IUBMB Comments
[E2 ubiquitin-conjugating enzyme]-S-ubiquitinyl-L-cysteine:[acceptor protein] ubiquitin transferase (isopeptide bond-forming; RING-type)
RING E3 ubiquitin transferases serve as mediators bringing the ubiquitin-charged E2 ubiquitin-conjugating enzyme (EC 2.3.2.23) and an acceptor protein together to enable the direct transfer of ubiquitin through the formation of an isopeptide bond between the C-terminal glycine residue of ubiquitin and the epsilon-amino group of an L-lysine residue of the acceptor protein. Unlike EC 2.3.2.26, HECT-type E3 ubiquitin transferase, the RING-E3 domain does not form a catalytic thioester intermediate with ubiquitin. Many members of the RING-type E3 ubiquitin transferase family are not able to bind a substrate directly, and form a complex with a cullin scaffold protein and a substrate recognition module (the complexes are named CRL for Cullin-RING-Ligase). In these complexes, the RING-type E3 ubiquitin transferase provides an additional function, mediating the transfer of a NEDD8 protein from a dedicated E2 carrier to the cullin protein (see EC 2.3.2.32, cullin-RING-type E3 NEDD8 transferase). cf. EC 2.3.2.31, RBR-type E3 ubiquitin transferase.
SUBSTRATE
PRODUCT                       
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate) hide
LITERATURE
(Substrate)
COMMENTARY
(Product) hide
LITERATURE
(Product)
Reversibility
r=reversible
ir=irreversible
?=not specified
[RNF180-ubiquitin-carrier protein UbcH6]-S-ubiquitinyl-L-cysteine + [Zic2]-L-lysine
[RNF180-ubiquitin-carrier protein UbcH6]-L-cysteine + [Zic2]-N6-ubiquitinyl-L-lysine
show the reaction diagram
Zic2, belongs to the Zic family nuclear zinc finger proteins
-
-
?
S-ubiquitinyl-[UbcH5a]-L-cysteine + [p21]-L-lysine
[UbcH5a]-L-cysteine + N6-ubiquitinyl-[p21]-L-lysine
show the reaction diagram
-
substrate p21 is a protein necessary for the proliferation of a subset of platelet-derived growth factor-transformed proneural glioma cells
UbcH5a is a preferred E2 enzyme for TRIM3-dependent p21 ubiquitination. Ubiquitination is practically eliminated in a p21 K15R/K74R/K91R/K136R quadruple mutant
-
?
[RNF220-ubiquitin-carrier protein]-S-ubiquitinyl-L-cysteine + [RF220]-L-lysine
[RNF220-ubiquitin-carrier protein]-L-cysteine + [RNF220]-N6-ubiquitinyl-L-lysine
show the reaction diagram
-
isoform RNF220 can bind ubiquitin-conjugating enzyme and mediate auto-ubiquitination of itself
-
?
[RNF220-ubiquitin-carrier protein]-S-ubiquitinyl-L-cysteine + [Sin3B]-L-lysine
[RNF220-ubiquitin-carrier protein]-L-cysteine + [Sin3B]-N6-ubiquitinyl-L-lysine
show the reaction diagram
Sin3B, a global regulator of gene transcription, which serves as an essential scaffold protein of the Sin3/HDAC corepressor complex
isoform RNF220 specifically interacts with Sin3B both in vitro and in vivo. Sin3B can be regulated by the ubiquitin-proteasome system. Co-expression of RNF220 and Sin3B promotes the ubiquitination and proteasomal degradation of Sin3B
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?
INHIBITOR
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
MLN4924
-
Nedd8 activating enzyme (NAE1) inhibitor, interferes with the activation of all cullin E3-ligases
ORGANISM
COMMENTARY hide
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
isoform RNF180
UniProt
Manually annotated by BRENDA team
SOURCE TISSUE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
SOURCE
of adult and developing animals, particularly in the ventricular layer of the cerebral cortex at embryonic stages
Manually annotated by BRENDA team
developing lens
Manually annotated by BRENDA team
-
primary myoblast cell
Manually annotated by BRENDA team
LOCALIZATION
ORGANISM
UNIPROT
COMMENTARY hide
GeneOntology No.
LITERATURE
SOURCE
integral membrane protein
Manually annotated by BRENDA team
nuclear envelope
Manually annotated by BRENDA team
the RING domain is required for proper cellular localization
Manually annotated by BRENDA team
GENERAL INFORMATION
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
physiological function
UNIPROT
ENTRY NAME
ORGANISM
NO. OF AA
NO. OF TRANSM. HELICES
MOLECULAR WEIGHT[Da]
SOURCE
SEQUENCE
LOCALIZATION PREDICTION?
RN180_MOUSE
592
1
67371
Swiss-Prot
other Location (Reliability: 1)
POSTTRANSLATIONAL MODIFICATION
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
ubiquitination
isoform RNF180 itself is heavily ubiquitinated and degraded by the proteasome
REF.
AUTHORS
TITLE
JOURNAL
VOL.
PAGES
YEAR
ORGANISM (UNIPROT)
PUBMED ID
SOURCE
Ogawa, M.; Mizugishi, K.; Ishiguro, A.; Koyabu, Y.; Imai, Y.; Takahashi, R.; Mikoshiba, K.; Aruga, J.
Rines/RNF180, a novel RING finger gene-encoded product, is a membrane-bound ubiquitin ligase
Genes Cells
13
397-409
2008
Mus musculus (Q3U827)
Manually annotated by BRENDA team
Kong, Q.; Zeng, W.; Wu, J.; Hu, W.; Li, C.; Mao, B.
RNF220, an E3 ubiquitin ligase that targets Sin3B for ubiquitination
Biochem. Biophys. Res. Commun.
393
708-713
2010
Mus musculus (Q6PDX6)
Manually annotated by BRENDA team
Raheja, R.; Liu, Y.; Hukkelhoven, E.; Yeh, N.; Koff, A.
The ability of TRIM3 to induce growth arrest depends on RING-dependent E3 ligase activity
Biochem. J.
458
537-545
2014
Mus musculus
Manually annotated by BRENDA team
Suisse, A.; Bekes, M.; Huang, T.T.; Treisman, J.E.
The COP9 signalosome inhibits Cullin-RING E3 ubiquitin ligases independently of its deneddylase activity
Fly
12
118-126
2018
Mus musculus
Manually annotated by BRENDA team