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

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Mus musculus


The taxonomic range for the selected organisms is: Mus musculus

The enzyme appears in selected viruses and cellular organisms

EC NUMBER
COMMENTARY hide
2.3.2.27
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RECOMMENDED NAME
GeneOntology No.
RING-type E3 ubiquitin transferase
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PATHWAY
BRENDA Link
KEGG Link
MetaCyc Link
protein ubiquitination
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SYSTEMATIC NAME
IUBMB Comments
[E2 ubiquitin-conjugating enzyme]-S-ubiquitinyl-L-cysteine:[acceptor protein] ubiquitin transferase (isopeptide bond-forming; RING-type)
The RING domain of E3 ubiquitin transferase serves as a mediator bringing the ubiquitin-charged E2 ubiquitin-conjugating enzyme and the 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 an the epsilon-amino group of an L-lysine residue of the acceptor protein. The RING-E3 domain does not form a catalytic thioester intermediate with ubiquitin (unlike the HECT domain, EC 2.3.2.26). RING-type ubiquitin transferases may occur as single-chain enzymes but also in dimeric forms or in multi-subunit assemblies.
ORGANISM
COMMENTARY hide
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
GENERAL INFORMATION
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
physiological function
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the RING domain is necessary for TRIM3-induced growth arrest of cells
SUBSTRATE
PRODUCT                       
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate) hide
LITERATURE
(Substrate)
COMMENTARY
(Product) hide
LITERATURE
(Product)
Reversibility
r=reversible
ir=irreversible
?=not specified
S-ubiquitinyl-[UbcH5a]-L-cysteine + [p21]-L-lysine
[UbcH5a]-L-cysteine + N6-ubiquitinyl-[p21]-L-lysine
show the reaction diagram
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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
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?
[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
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?
[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
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isoform RNF220 can bind ubiquitin-conjugating enzyme and mediate auto-ubiquitination of itself
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?
[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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?
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
LOCALIZATION
ORGANISM
UNIPROT
COMMENTARY hide
GeneOntology No.
LITERATURE
SOURCE
the RING domain is required for proper cellular localization
Manually annotated by BRENDA team
integral membrane protein
Manually annotated by BRENDA team
nuclear envelope
Manually annotated by BRENDA team
PDB
SCOP
CATH
UNIPROT
ORGANISM
Mus musculus;
POSTTRANSLATIONAL MODIFICATION
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
ubiquitination
isoform RNF180 itself is heavily ubiquitinated and degraded by the proteasome
Show AA Sequence (218 entries)
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