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Information on EC 2.3.2.26 - HECT-type E3 ubiquitin transferase and Organism(s) Arabidopsis thaliana and UniProt Accession Q9SU29

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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Arabidopsis thaliana
UNIPROT: Q9SU29
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The taxonomic range for the selected organisms is: Arabidopsis thaliana
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
PATHWAY SOURCE
PATHWAYS
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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
[ubiquitin-conjugating enzyme E2]-S-ubiquitin-L-cysteine + [transcription factor WRKY53]-L-lysine
[ubiquitin-conjugating enzyme E2D3]-L-cysteine + [transcription factor WRKY53]-N6-ubiquitinyl-L-lysine
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UPL5 is able to use the WRKY53 protein as a substrate for polyubiquitination in an in vitro system, and induction of UPL5 expression by an ethanol-inducible system in upl5 plants leads to degradation of the WRKY53 protein
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?
additional information
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isoform UPL5 interacts with transcription factor WRKY53 via its leucine zipper domain
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?
ORGANISM
COMMENTARY hide
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
isoform UPL5
UniProt
Manually annotated by BRENDA team
GENERAL INFORMATION
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
physiological function
isoform UPL5 T-DNA insertion lines show the same senescence phenotype as transcription factor WRKY53 over-expressers. Over-expression of WRKY53 in the upl5 background enhances the accelerated senescence phenotype of WRKY53 over-expressers
physiological function
T-DNA disruptions of the UPL3 locus do not affect overall growth and morphology, but display aberrant trichome morphology. Many mutant trichomes contain five or more branches instead of three branches. Mutant trichoimes often undergo an additional round of endoreplication resulting in enlarged nuclei with ploidy levels of up to 64C. Mutant plants are hypersensitive to gibberellic acid-3. The phenotype of upl3 mutants is similar to that of kaktus, a set of trichome mutants with supernumerary branches. UPL3 mutants and kaktus-2 are allelic with kaktus-2 plants harboring a splice-site mutation within the UPL3-transcribed region
UNIPROT
ENTRY NAME
ORGANISM
NO. OF AA
NO. OF TRANSM. HELICES
MOLECULAR WEIGHT[Da]
SOURCE
SEQUENCE
LOCALIZATION PREDICTION?
UPL5_ARATH
873
0
100365
Swiss-Prot
other Location (Reliability: 2)
EXPRESSION
ORGANISM
UNIPROT
LITERATURE
UPL5 expression is reduced after hydrogen peroxide treatment
UPL5 is highly expressed in leaf tissue but expression is reduced at bolting when transcription factor WRKY53 protein levels should be high
UPL5 is induced by jasmonic acid treatment
REF.
AUTHORS
TITLE
JOURNAL
VOL.
PAGES
YEAR
ORGANISM (UNIPROT)
PUBMED ID
SOURCE
Miao, Y.; Zentgraf, U.
A HECT E3 ubiquitin ligase negatively regulates Arabidopsis leaf senescence through degradation of the transcription factor WRKY53
Plant J.
63
179-188
2010
Arabidopsis thaliana (Q9SU29)
Manually annotated by BRENDA team
Downes, B.P.; Stupar, R.M.; Gingerich, D.J.; Vierstra, R.D.
The HECT ubiquitin-protein ligase (UPL) family in Arabidopsis: UPL3 has a specific role in trichome development
Plant J.
35
729-742
2003
Arabidopsis thaliana (Q6WWW4)
Manually annotated by BRENDA team