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Information on EC 2.3.2.B12 - ubiquitin transferase U-box E4 and Organism(s) Saccharomyces cerevisiae and UniProt Accession P54860

for references in articles please use BRENDA:EC2.3.2.B12
preliminary BRENDA-supplied EC number
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EC Tree
     2 Transferases
         2.3 Acyltransferases
             2.3.2 Aminoacyltransferases
                2.3.2.B12 ubiquitin transferase U-box E4
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This record set is specific for:
Saccharomyces cerevisiae
UNIPROT: P54860 not found.
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The taxonomic range for the selected organisms is: Saccharomyces cerevisiae
The expected taxonomic range for this enzyme is: Eukaryota, Bacteria
Reaction Schemes
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S-ubiquitinyl-[U-box-E4-ubiquitin-carrier protein]-L-cysteine
+
N6-ubiquitinyl-[acceptor protein]-L-lysine
=
[U-box-E4-ubiquitin-carrier protein]-L-cysteine
+
N6-[N6-ubiquitinyl-L-lysyl]-ubiquitinyl-[acceptor protein]-L-lysine
S-ubiquitinyl-[U-box-E4-ubiquitin-carrier protein]-L-cysteine
+
N6-ubiquitinyl-[acceptor protein]-L-lysine
=
[U-box-E4-ubiquitin-carrier protein]-L-cysteine
+
N6-[N6-ubiquitinyl-L-lysyl]-ubiquitinyl-[acceptor protein]-L-lysine
S-ubiquitinyl-[U-box-E4-ubiquitin-carrier protein]-L-cysteine
+
N6-ubiquitinyl-[acceptor protein]-L-lysine
=
[U-box-E4-ubiquitin-carrier protein]-L-cysteine
+
N6-(N6-ubiquitinyl-L-lysyl)-ubiquitinyl-[acceptor protein]-L-lysine
S-ubiquitinyl-[U-box-E4-ubiquitin-carrier protein]-L-cysteine
+
N6-ubiquitinyl-[acceptor protein]-L-lysine
=
[U-box-E4-ubiquitin-carrier protein]-L-cysteine
+
N6-(N6-ubiquitinyl-L-lysyl)-ubiquitinyl-[acceptor protein]-L-lysine
Synonyms
ufd2a, e4 ubiquitin ligase, muse3, e4 ligase, ubiquitin fusion degradation protein 2, more
SYNONYM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
E4 ubiquitin-protein ligase UFD2
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ubiquitin conjugation factor E4
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ubiquitin fusion degradation protein 2
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ubiquitin chain elongation enzyme Ufd2
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Ubr1-dependent E4 enzyme
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Ufd2
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founding member of the E4 enzymes, belongs to a family containing a conserved U-box motif
Ufd4-enhancing ubiquitiylation enzyme
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REACTION
REACTION DIAGRAM
COMMENTARY hide
ORGANISM
UNIPROT
LITERATURE
S-ubiquitinyl-[U-box-E4-ubiquitin-carrier protein]-L-cysteine + N6-ubiquitinyl-[acceptor protein]-L-lysine = [U-box-E4-ubiquitin-carrier protein]-L-cysteine + N6-(N6-ubiquitinyl-L-lysyl)-ubiquitinyl-[acceptor protein]-L-lysine
show the reaction diagram
E4 used to describe an E3 when it enhances ubiquitin chain elongation and potentialy also forms additional chains
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SYSTEMATIC NAME
IUBMB Comments
[U-box-E4-ubiquitin-carrier protein]-S-ubiquitinyl-L-cysteine:acceptor protein-ubiquitinyl ubiquitin transferase (isopeptide bond-forming)
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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-[U-box-E4-ubiquitin-carrier protein]-L-cysteine + N6-ubiquitinyl-[acceptor protein]-L-lysine
[U-box-E4-ubiquitin-carrier protein]-L-cysteine + N6-[N6-ubiquitinyl-L-lysyl]-ubiquitinyl-[acceptor protein]-L-lysine
show the reaction diagram
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?
additional information
?
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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
additional information
?
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the U-box domain is essentiel for the involvement of Ufd2 in Pex29 degradation. Pex29 is a peroxiisomal membrane protein that regulates the number and size of peroxisomes. Pex29 is regulated by ubiquitin-protein E3 ligase. Further extension of the growing ubiquitin chain requires assistance of Ufd2 due to the spatial positioning of the E3 and its substrate. Ufd2 elongates Pex29 with predominatly Lys48-linked ubiquitin chain in vivo
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?
ORGANISM
COMMENTARY hide
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
GENERAL INFORMATION
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
physiological function
Ufd2 catalyses K48-linked multi-monoubiquitination on K29-linked ubiquitin chains assembled by the ubiquitin ligase Ufd4, resulting in branched ubiquitin chains. The reaction depends on the interaction of K29-linked ubiquitin chains with two N-terminal loops of Ufd2. Only following the addition of K48-linked ubiquitin to substrates modified with K29-linked ubiquitin chains, the substrates can be escorted to the proteasome for degradation. This ubiquitin chain linkage switching reaction is essential for ERAD, oleic acid and acid pH resistance in yeast
physiological function
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E4 is an additional factor working together with ubiquitin-activating enzyme E1, ubiquitin-conjugating enzyme E2, and ubiquitin transferase E3, in some cases specifically required for multiubiquitin chain polymerization, a function attributed to Ufd2, the first protein designated as an E4
CRYSTALLIZATION (Commentary)
ORGANISM
UNIPROT
LITERATURE
crystal structure of Ufd2 in complex with the ubiquitin-like (UBL) and ubiquitin-associated (UBA) proteins Rad23 and Dsk2 domains, PDB-ID: 3M62 and 3M63, respectively. The structure of Ufd2 is solved in complex with Rad23-UBL carrying either an N-terminal or a C-terminal His tag, refined at 2.4 A resolution. Ufd2 is composed of an N-terminal variable domain, a core domain, and a C-termional U-box with a fold similar to that of RING. The structure of Ufd2 with Dsk2-UBL is solved by molecular replacement. THe structure exhibits increased flexibility, in particular with a C-terminally tagged UBL domain. The N-terminal, tagged protein structure is refined at 2.4 A resolution. The N-terminal UBL-binding region of yeast Ufd2 is conserved on lower eukaryotes
PURIFICATION (Commentary)
ORGANISM
UNIPROT
LITERATURE
REF.
AUTHORS
TITLE
JOURNAL
VOL.
PAGES
YEAR
ORGANISM (UNIPROT)
PUBMED ID
SOURCE
Liu, C; van Dyk, D.; Xu, P.; Choe, V.; Pan, H.; Peng, J.; Andrews, B.; Rao, H.
Ubiquitin chain elongation enzyme Ufd2 regulates a subset of Doa10 substrates
J. Biol. Chem.
285
10265-10272
2010
Saccharomyces cerevisiae, Saccharomyces cerevisiae ATCC 204508
Manually annotated by BRENDA team
Hnzelmann, P.; Stingele, J.; Hofmann, K.; Schindelin, H.; Raasi, S.
The yeast E4 ubiquitin ligase Ufd2 interacts with the ubiquitin-like domains of Rad23 and Dsk2 via a novel and distinct ubiquitin-like binding domain
J. Biol. Chem.
285
20390-20398
2010
Saccharomyces cerevisiae (P54860), Saccharomyces cerevisiae, Saccharomyces cerevisiae ATCC 204508 (P54860)
Manually annotated by BRENDA team
Metzger, M.B.; Weissman, A.M.;
Working on a chain: E3s ganging up for ubiquitylation
Nat. Cell Biol.
12
1124-1126
2010
Saccharomyces cerevisiae
Manually annotated by BRENDA team
Liu, C.; Liu, W.; Ye, Y.; Li, W.
Ufd2p synthesizes branched ubiquitin chains to promote the degradation of substrates modified with atypical chains
Nat. Commun.
8
14274
2017
Saccharomyces cerevisiae (P54860)
Manually annotated by BRENDA team