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Information on EC 2.3.2.26 - HECT-type E3 ubiquitin transferase and Organism(s) Mus musculus and UniProt Accession Q80TP3

for references in articles please use BRENDA:EC2.3.2.26
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EC Tree
     2 Transferases
         2.3 Acyltransferases
             2.3.2 Aminoacyltransferases
                2.3.2.26 HECT-type E3 ubiquitin transferase
IUBMB Comments
In the first step the enzyme transfers ubiquitin from the E2 ubiquitin-conjugating enzyme (EC 2.3.2.23) to a cysteine residue in its HECT domain (which is located in the C-terminal region), forming a thioester bond. In a subsequent step the enzyme transfers the ubiquitin to an acceptor protein, resulting in 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. cf. EC 2.3.2.27, RING-type E3 ubiquitin transferase and EC 2.3.2.31, RBR-type E3 ubiquitin transferase.
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This record set is specific for:
Mus musculus
UNIPROT: Q80TP3
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The taxonomic range for the selected organisms is: Mus musculus
The expected taxonomic range for this enzyme is: Eukaryota, Bacteria, Archaea
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
nedd4, smurf1, smurf2, huwe1, nedd4l, nedd4-1, e6-ap, ube3c, trp120, trip12, more
SYNONYM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
HECT domain E3 ubiquitin ligase
-
-
HECT-type E3 ligase
-
-
HECT-type ubiquitin E3 ligase
-
-
Itch
-
-
TRIP12
-
-
PATHWAY SOURCE
PATHWAYS
-
-
SYSTEMATIC NAME
IUBMB Comments
[E2 ubiquitin-conjugating enzyme]-S-ubiquitinyl-L-cysteine:[acceptor protein] ubiquitin transferase (isopeptide bond-forming)
In the first step the enzyme transfers ubiquitin from the E2 ubiquitin-conjugating enzyme (EC 2.3.2.23) to a cysteine residue in its HECT domain (which is located in the C-terminal region), forming a thioester bond. In a subsequent step the enzyme transfers the ubiquitin to an acceptor protein, resulting in 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. cf. EC 2.3.2.27, RING-type E3 ubiquitin transferase and 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
S-ubiquitinyl-[HECT-type E3 ubiquitin transferase]-L-cysteine + [Sox6 protein]-L-lysine
[HECT-type E3 ubiquitin transferase]-L-cysteine + N6-ubiquitinyl-[Sox6 protein]-L-lysine
show the reaction diagram
-
-
-
-
?
[E2 ubiquitin-conjugating enzyme]-S-ubiquitinyl-L-cysteine + [my-opioid receptor MOR1]-L-lysine
[E2 ubiquitin-conjugating enzyme]-L-cysteine + [my-opioid receptor MOR1]-N6-ubiquitinyl-L-lysine
show the reaction diagram
-
-
-
?
NATURAL SUBSTRATE
NATURAL PRODUCT
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate) hide
LITERATURE
(Substrate)
COMMENTARY
(Product) hide
LITERATURE
(Product)
REVERSIBILITY
r=reversible
ir=irreversible
?=not specified
S-ubiquitinyl-[HECT-type E3 ubiquitin transferase]-L-cysteine + [Sox6 protein]-L-lysine
[HECT-type E3 ubiquitin transferase]-L-cysteine + N6-ubiquitinyl-[Sox6 protein]-L-lysine
show the reaction diagram
-
-
-
-
?
ORGANISM
COMMENTARY hide
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
isoform UBR5
UniProt
Manually annotated by BRENDA team
LOCALIZATION
ORGANISM
UNIPROT
COMMENTARY hide
GeneOntology No.
LITERATURE
SOURCE
enzyme UBR5 localizes in the nuclei of smooth muscle cells and forms a complex with myocardin in vivo and in vitro
Manually annotated by BRENDA team
GENERAL INFORMATION
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
physiological function
ubiquitin ligase UBR5 specifically enhances trans-activation of smooth muscle-specific promoters by the myocardin family of proteins. UBR5 significantly augments the ability of myocardin to induce expression of endogenous smooth muscle cell marker genes independent on its E3 ligase function. Depletion of endogenous UBR5 by small interfering RNA in fibroblast cells attenuates myocardin-induced smooth muscle-specific gene expression, and UBR5 knockdown in smooth muscle cells results in down-regulation of smooth muscle-specific genes. UBR5 can attenuate myocardin protein degradation resulting in increased myocardin protein expression without affecting myocardin mRNA expression. The effects of UBR5 on myocardin requires only the HECT and UBR1 domains of UBR5
malfunction
physiological function
UNIPROT
ENTRY NAME
ORGANISM
NO. OF AA
NO. OF TRANSM. HELICES
MOLECULAR WEIGHT[Da]
SOURCE
SEQUENCE
LOCALIZATION PREDICTION?
UBR5_MOUSE
2792
0
308352
Swiss-Prot
other Location (Reliability: 1)
MOLECULAR WEIGHT
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
113000
-
x * 113000, SDS-PAGE
200000
-
x * 200000, SDS-PAGE
SUBUNIT
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
EXPRESSION
ORGANISM
UNIPROT
LITERATURE
enzyme expression is increased 3 h after Dox stimulation (0.0005 mM)
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REF.
AUTHORS
TITLE
JOURNAL
VOL.
PAGES
YEAR
ORGANISM (UNIPROT)
PUBMED ID
SOURCE
Hu, G.; Wang, X.; Saunders, D.; Henderson, M.; Russell, A.; Herring, B.; Zhou, J.
Modulation of myocardin function by the ubiquitin E3 ligase UBR5
J. Biol. Chem.
286
11800-11809
2011
Mus musculus (Q80TP3)
Manually annotated by BRENDA team
Otaki, Y.; Takahashi, H.; Watanabe, T.; Funayama, A.; Netsu, S.; Honda, Y.; Narumi, T.; Kadowaki, S.; Hasegawa, H.; Honda, S.; Arimoto, T.; Shishido, T.; Miyamoto, T.; Kamata, H.; Nakajima, O.; Kubota, I.
HECT-type ubiquitin E3 ligase ITCH interacts with thioredoxin-interacting protein and ameliorates reactive oxygen species-induced cardiotoxicity
J. Am. Heart Assoc.
5
e002485
2016
Mus musculus, Rattus norvegicus
Manually annotated by BRENDA team
An, C.I.; Ganio, E.; Hagiwara, N.
Trip12, a HECT domain E3 ubiquitin ligase, targets Sox6 for proteasomal degradation and affects fiber type-specific gene expression in muscle cells
Skeletal Muscle
3
11
2013
Homo sapiens (Q14669), Mus musculus
Manually annotated by BRENDA team
Dong, S.; Liu, J.; Li, L.; Wang, H.; Ma, H.; Zhao, Y.; Zhao, J.
The HECT ubiquitin E3 ligase Smurf2 degrades my-opioid receptor 1 in the ubiquitin-proteasome system in lung epithelial cells
Am. J. Physiol. Cell Physiol.
316
C632-C640
2019
Mus musculus (A2A5Z6)
Manually annotated by BRENDA team