Information on EC 2.3.2.B12 - ubiquitin transferase U-box E4

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The enzyme appears in viruses and cellular organisms

EC NUMBER
COMMENTARY hide
2.3.2.B12
preliminary BRENDA-supplied EC number
RECOMMENDED NAME
GeneOntology No.
ubiquitin transferase U-box E4
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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
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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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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ORGANISM
COMMENTARY hide
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
GENERAL INFORMATION
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
evolution
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MUSE3 is a single copy gene encoding a ubiquitin-conjugating E4 factor with a conserved Ub-elongating factor core domain (UFD2p core domain) and a C-terminal U-box domain. Phylogenetic analysis shows that MUSE3 is a highly conserved protein in all sequenced eukaryotes
physiological function
SUBSTRATE
PRODUCT                       
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate) hide
LITERATURE
(Substrate)
COMMENTARY
(Product) hide
LITERATURE
(Product)
Reversibility
r=reversible
ir=irreversible
?=not specified
[CHIP U-box-E4-ubiquitin-carrier protein Ubc4]-S-ubiquitinyl-L-cysteine + [acceptor protein]-N6-ubiquitinyl-L-lysine
[CHIP U-box-E4-ubiquitin-carrier protein Ubc4]-L-cysteine + [acceptor protein]-N6-ubiquitinyl-ubiquitinyl-L-lysine
show the reaction diagram
AI390103, Q9ES00, Q9WUD1
enzyme mediates polyubiquitination in the presence of E1 and E2 and in the absence of E3, exhibiting different specificities for E2 enzymes. Ubiquination activity of CHIP is greatest with E2 enzymes Ubc4 or UbcH5C
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[CHIP U-box-E4-ubiquitin-carrier protein UbH5C4]-S-ubiquitinyl-L-cysteine + [acceptor protein]-N6-ubiquitinyl-L-lysine
[CHIP U-box-E4-ubiquitin-carrier protein UbcH5C]-L-cysteine + [acceptor protein]-N6-ubiquitinyl-ubiquitinyl-L-lysine
show the reaction diagram
AI390103, Q9ES00, Q9WUD1
enzyme mediates polyubiquitination in the presence of E1 and E2 and in the absence of E3, exhibiting different specificities for E2 enzymes. Ubiquination activity of CHIP is greatest with E2 enzymes Ubc4 or UbcH5C
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[CYC4 U-box-E4-ubiquitin-carrier protein Ubc2B]-S-ubiquitinyl-L-cysteine + [acceptor protein]-N6-ubiquitinyl-L-lysine
[CYC4 U-box-E4-ubiquitin-carrier protein Ubc2B]-L-cysteine + [acceptor protein]-N6-ubiquitinyl-ubiquitinyl-L-lysine
show the reaction diagram
HSU37219, XM006045
enzyme mediates polyubiquitination in the presence of E1 and E2 and in the absence of E3, exhibiting different specificities for E2 enzymes. Ubiquination activity of CYC4 is greatest with E2 enzymes Ubc2B or Ubc3, but is also activ with UbcH7
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[CYC4 U-box-E4-ubiquitin-carrier protein Ubc3]-S-ubiquitinyl-L-cysteine + [acceptor protein]-N6-ubiquitinyl-L-lysine
[CYC4 U-box-E4-ubiquitin-carrier protein Ubc3]-L-cysteine + [acceptor protein]-N6-ubiquitinyl-ubiquitinyl-L-lysine
show the reaction diagram
HSU37219, XM006045
enzyme mediates polyubiquitination in the presence of E1 and E2 and in the absence of E3, exhibiting different specificities for E2 enzymes. Ubiquination activity of CYC4 is greatest with E2 enzymes Ubc2 or Ubc3, but is also activ with UbcH7
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[CYC4 U-box-E4-ubiquitin-carrier protein UbcH7]-S-ubiquitinyl-L-cysteine + [acceptor protein]-N6-ubiquitinyl-L-lysine
[CYC4 U-box-E4-ubiquitin-carrier protein UbcH7]-L-cysteine + [acceptor protein]-N6-ubiquitinyl-ubiquitinyl-L-lysine
show the reaction diagram
HSU37219, XM006045
enzyme mediates polyubiquitination in the presence of E1 and E2 and in the absence of E3, exhibiting different specificities for E2 enzymes. Ubiquination activity of CYC4 is greatest with E2 enzymes Ubc2 or Ubc3, but is also activ with UbcH7
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[p300/CREB-binding protein U-box-E4-ubiquitin-carrier protein]-S-ubiquitinyl-L-cysteine + [acceptor p53]-N6-ubiquitinyl-L-lysine
[p300/CREB-binding protein U-box-E4-ubiquitin-carrier protein]-L-cysteine + [acceptor p53]-N6-ubiquitinyl-ubiquitinyl-L-lysine
show the reaction diagram
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both p300 and CREB-binding protein are required for endogenous p53 polyubiquitination and the normally rapid turnover of p53 in unstressed cells. CREB-binding protein deficiency specifically stabilizes cytoplasmic, but not nuclear p53. The N-terminal 616 aa of CREB-binding protein, which includes the conserved Zn2+-binding C/H1-TAZ1 domain, is the minimal domain sufficient to destabilize p53 in vivo
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[PRP19 U-box-E4-ubiquitin-carrier protein Ubc3]-S-ubiquitinyl-L-cysteine + [acceptor protein]-N6-ubiquitinyl-L-lysine
[PRP19 U-box-E4-ubiquitin-carrier protein Ubc3]-L-cysteine + [acceptor protein]-N6-ubiquitinyl-ubiquitinyl-L-lysine
show the reaction diagram
HSU37219, XM006045
enzyme mediates polyubiquitination in the presence of E1 and E2 and in the absence of E3, exhibiting different specificities for E2 enzymes. Ubiquination activity of PRP19 is greatest with E2 enzyme Ubc3
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[UFD2a U-box-E4-ubiquitin-carrier protein Ubc4]-S-ubiquitinyl-L-cysteine + [acceptor protein]-N6-ubiquitinyl-L-lysine
[U-box-E4-ubiquitin-carrier protein]-L-cysteine + [acceptor protein]-N6-ubiquitinyl-ubiquitinyl-L-lysine
show the reaction diagram
AI390103, Q9ES00, Q9WUD1
enzyme mediates polyubiquitination in the presence of E1 and E2 and in the absence of E3, exhibiting different specificities for E2 enzymes. Ubiquination activity of UFD2a is greatest with E2 enzymes Ubc4 or UbcH5C
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[UFD2b U-box-E4-ubiquitin-carrier protein Ubc4]-S-ubiquitinyl-L-cysteine + [acceptor protein]-N6-ubiquitinyl-L-lysine
[UFD2b U-box-E4-ubiquitin-carrier protein Ubc4]-L-cysteine + [acceptor protein]-N6-ubiquitinyl-ubiquitinyl-L-lysine
show the reaction diagram
AI390103, Q9ES00, Q9WUD1
enzyme mediates polyubiquitination in the presence of E1 and E2 and in the absence of E3, exhibiting different specificities for E2 enzymes. Ubiquination activity of UFD2b is greatest with E2 enzymes Ubc4 or UbcH5C
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[UFD2b U-box-E4-ubiquitin-carrier protein UbH5C]-S-ubiquitinyl-L-cysteine + [acceptor protein]-N6-ubiquitinyl-L-lysine
[UFD2b U-box-E4-ubiquitin-carrier protein UbcH5C]-L-cysteine + [acceptor protein]-N6-ubiquitinyl-ubiquitinyl-L-lysine
show the reaction diagram
AI390103, Q9ES00, Q9WUD1
enzyme mediates polyubiquitination in the presence of E1 and E2 and in the absence of E3, exhibiting different specificities for E2 enzymes. Ubiquination activity of UFD2b is greatest with E2 enzymes Ubc4 or UbcH5C
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additional information
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NATURAL SUBSTRATES
NATURAL PRODUCTS
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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SOURCE TISSUE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
SOURCE
AI390103, Q9ES00, Q9WUD1
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Manually annotated by BRENDA team
HSU37219, XM006045
;
Manually annotated by BRENDA team
HSU37219, XM006045
;
Manually annotated by BRENDA team
HSU37219, XM006045
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Manually annotated by BRENDA team
AI390103, Q9ES00, Q9WUD1
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Manually annotated by BRENDA team
LOCALIZATION
ORGANISM
UNIPROT
COMMENTARY hide
GeneOntology No.
LITERATURE
SOURCE
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
Cloned/COMMENTARY
ORGANISM
UNIPROT
LITERATURE
expression in HeLa cell, Escherichia coli; expression in HeLa cell, Escherichia coli
HSU37219, XM006045
expression in HeLa cell, Escherichia coli; expression in HeLa cell, Escherichia coli; expression in HeLa cell, Escherichia coli
AI390103, Q9ES00, Q9WUD1
expression in JHU-022 cell and H-1299 cell
ENGINEERING
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
P1140A
AI390103, Q9ES00, Q9WUD1
mutation of the conserved proline residue, abolishes E3 activity of isoform UFD2a
P270A
AI390103, Q9ES00, Q9WUD1
loss of polyubiquitination activity
additional information
APPLICATION
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
medicine
DELTANp63alpha, dominant negative isoform of the p63 family and essential survival factor in head and neck squamous cell carcinoma, physically interacts with U-box-type E4 ubiquitin ligase UFD2a. UFD2a stabilizes DELTANp63alpha, and ubiquitylation of DELTANp63?alpha is attenuated by UFD2a both in the presence and absence of cisplatin. Ectopic expression of UFD2a increases the half-life of DELTANp63alpha in association with a significant enhancement of the repressive transcriptional activity of DELTANp63alpha. Downregulation of endogenous UFD2a by RNAi results in degradation of DELTANp63alpha