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Information on EC 2.3.2.B12 - ubiquitin transferase U-box E4
for references in articles please use BRENDA:EC2.3.2.B12preliminary BRENDA-supplied EC number
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EC Tree
2.3.2.B12 ubiquitin transferase U-box E4Specify your search results
Word Map
The expected taxonomic range for this enzyme is: Eukaryota, Bacteria
Reaction Schemes
+
=
+
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
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SYNONYM 
ORGANISM
UNIPROT
COMMENTARY 
LITERATURE
E4 ubiquitin-protein ligase UFD2
ubiquitin chain elongation enzyme Ufd2
ubiquitin conjugation factor E4
ubiquitin fusion degradation protein 2
Ufd2
Ufd2a
Ufd2
-
founding member of the E4 enzymes, belongs to a family containing a conserved U-box motif
Ufd2
-
founding member of the E4 enzymes, belongs to a family containing a conserved U-box motif
-
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REACTION
REACTION DIAGRAM
COMMENTARY
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
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
E4 used to describe an E3 when it enhances ubiquitin chain elongation and potentialy also forms additional chains
-
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
-
-
-
-
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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)
(Substrate)
LITERATURE
(Substrate)
(Substrate)
COMMENTARY
(Product)
(Product)
LITERATURE
(Product)
(Product)
Reversibility
r=reversible
ir=irreversible
?=not specified
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
-
-
-
?
[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
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
-
-
?
[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
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
-
-
?
[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
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
-
-
?
[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
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
-
-
?
[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
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
-
-
?
[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
-
-
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
-
?
[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
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
-
-
?
[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
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
-
-
?
[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
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
-
-
?
[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
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
-
-
?
additional information
?
-
-
MUSE3 functions as an E4 factor and works downstream of the E3 ligase SCFCPR1 to facilitate the polyubiquitination and degradation of Resistance proteins, including SNC1 (Supressor of NPR1, Constitutive 1) and RPS2 (Resistance to Pseudomonas syringae 2)
-
-
?
additional information
?
-
HSU37219
data suggest that U box proteins constitute a third family of E3 enzymes and that E4 activity may reflect a specialized type of E3 activity. enzyme is able to catalyze ubiquitin chain formation on artificial substrates in the presence of E1 and E2 and in the absence of E3
-
-
?
additional information
?
-
XM006045
data suggest that U box proteins constitute a third family of E3 enzymes and that E4 activity may reflect a specialized type of E3 activity. enzyme is able to catalyze ubiquitin chain formation on artificial substrates in the presence of E1 and E2 and in the absence of E3
-
-
?
additional information
?
-
AI390103
data suggest that U box proteins constitute a third family of E3 enzymes and that E4 activity may reflect a specialized type of E3 activity. enzyme is able to catalyze ubiquitin chain formation on artificial substrates in the presence of E1 and E2 and in the absence of E3
-
-
?
additional information
?
-
data suggest that U box proteins constitute a third family of E3 enzymes and that E4 activity may reflect a specialized type of E3 activity. enzyme is able to catalyze ubiquitin chain formation on artificial substrates in the presence of E1 and E2 and in the absence of E3
-
-
?
additional information
?
-
data suggest that U box proteins constitute a third family of E3 enzymes and that E4 activity may reflect a specialized type of E3 activity. enzyme is able to catalyze ubiquitin chain formation on artificial substrates in the presence of E1 and E2 and in the absence of E3
-
-
?
additional information
?
-
-
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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-
?
additional information
?
-
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one target of Ufd2 is identified as Pex29, the ubiquitin-protein conjugate ubiquitinylated by the ubiquitin-protein E3 ligase Doa10. Not all Doa10 substrates are regulated by Ufd2, suggesting that E4 involvement is not specific to a particular E3, but might depend on the spatial arrangement of the E3-substrate interaction
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?
additional information
?
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Ufd4-enhancing ubiquitinylation of N-end rule substrates, Lys48 ubiquitin-chain formation and proteasomal degradation
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-
?
additional information
?
-
-
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
-
-
?
additional information
?
-
-
one target of Ufd2 is identified as Pex29, the ubiquitin-protein conjugate ubiquitinylated by the ubiquitin-protein E3 ligase Doa10. Not all Doa10 substrates are regulated by Ufd2, suggesting that E4 involvement is not specific to a particular E3, but might depend on the spatial arrangement of the E3-substrate interaction
-
-
?
additional information
?
-
the StoD C terminus is a U-box E3 ubiquitin ligase, capable of autoubiquitination in the presence of multiple E2 enzymes
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-
-
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NATURAL SUBSTRATE
NATURAL PRODUCT
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate)
(Substrate)
LITERATURE
(Substrate)
(Substrate)
COMMENTARY
(Product)
(Product)
LITERATURE
(Product)
(Product)
REVERSIBILITY
r=reversible
ir=irreversible
?=not specified
r=reversible
ir=irreversible
?=not specified
additional information
?
-
-
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
-
-
?
additional information
?
-
-
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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DISEASE
TITLE OF PUBLICATION
LINK TO PUBMED
Neuroblastoma
UFD2a mediates the proteasomal turnover of p73 without promoting p73 ubiquitination.
Neurodegenerative Diseases
Mammalian E4 is required for cardiac development and maintenance of the nervous system.
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ORGANISM
COMMENTARY
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
crystallization: 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; S288c
SwissProt
brenda
crystallization: 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; S288c
SwissProt
brenda
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SOURCE TISSUE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
SOURCE
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LOCALIZATION
ORGANISM
UNIPROT
COMMENTARY
GeneOntology No.
LITERATURE
SOURCE
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GENERAL INFORMATION
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
evolution
-
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
physiological function
-
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
physiological function
-
MUSE3 functions as an E4 factor and works downstream of the E3 ligase SCFCPR1 to facilitate the polyubiquitination and degradation of Resistance proteins, including SNC1 (Supressor of NPR1, Constitutive 1) and RPS2 (Resistance to Pseudomonas syringae 2)
physiological function
-
both coactivators p300 and CREB-binding protein are required for endogenous p53 polyubiquitination and the normally rapid turnover of p53 in unstressed cells. p300/CREB-binding protein ubiquitin ligase activities are absent in nuclear extracts and exclusively cytoplasmic. Consistent with the cytoplasmic localization of its E3/E4 activity, 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, and it includes within an intrinsic E3 autoubiquitination activity and, in a two-step E4 assay, exhibits robust E4 activity for p53
physiological function
DELTANp63alpha, dominant negative isoform of the p63 family, 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 DELTA?Np63alpha in association with a significant enhancement of the repressive transcriptional activity of DELTANp63alpha. Downregulation of endogenous UFD2a by RNAi results in degradation of DELTANp63alpha
physiological function
StoD is a type III secretion systems effector. In HeLa cells expressing StoD, ubiquitin is redistributed into puncta that colocalize with StoD. StoD N- and StoD C-terminus bind the same exposed surface of the beta-sheet of ubiquitin. StoD interacts with both K63- and K48-linked diubiquitin
physiological function
Ube4A is required for complete assembly of specific DNA damage repair factors at double-strand break sites and proper internal organization of double-strand break-associated protein foci. UBE4A's recruitment to sites of DNA damage is dependent on primary E3 ligases in the DNA damage repair and promotes enhancement and sustainment of K48- and K63-linked ubiquitin chains at these sites. This step is required for timely recruitment of the RAP80 and BRCA1 proteins and proper organization of RAP80- and BRCA1-associated protein complexes at double-strand break sites. The pathway is required for optimal end-resection at double-strand breaks, and its abrogation leads to up-regulation of the highly mutagenic alternative end-joining repair at the expense of error-free homologous recombination repair
physiological function
UFD-2 is a mediator of DNA-damage-induced apoptosis. After initiation of homologous recombination by RAD-51, UFD-2 forms foci that contain substrate-processivity factors including the ubiquitin-selective segregase CDC-48 (p97), the deubiquitination enzyme ATX-3 (Ataxin-3) and the proteasome. In the absence of UFD-2, RAD-51 foci persist, and DNA damage-induced apoptosis is prevented. UFD-2 foci are retained until recombination intermediates are removed by the Holliday-junction-processing enzymes GEN-1, MUS-81 or XPF-1. Formation of UFD-2 foci also requires proapoptotic CEP-1 (p53) signaling
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
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UNIPROT
ENTRY NAME
ORGANISM
NO. OF AA
NO. OF TRANSM. HELICES
MOLECULAR WEIGHT[Da]
SOURCE
SEQUENCE
LOCALIZATION PREDICTION
The reliability class of the localization prediction ranges from 1 (very reliable) to 5 (not reliable).
The reliability class of the localization prediction ranges from 1 (very reliable) to 5 (not reliable). UFD2_YEAST
Saccharomyces cerevisiae (strain ATCC 204508 / S288c)
961
0
109916
Swiss-Prot
-
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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
structure of the StoD N terminus at 2.5 A resolution reveals a ubiquitin-like fold
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PROTEIN VARIANTS
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
P1140A
mutation of the conserved proline residue, abolishes E3 activity of isoform UFD2a
additional information
additional information
-
mutations of MUSE3, muse3-1 and muse3-2 show enhanced resistance against the virulent oomycete Hyaloperonospora arabidopsidis Noco2 or the bacterial pathogen Pseudomonas syringae pv maculicola ES4326
additional information
AI390103
deletion of the U-box domain abolishes E3 activity of isoform UFD2a
additional information
deletion of the U-box domain abolishes E3 activity of isoform UFD2a
additional information
deletion of the U-box domain abolishes E3 activity of isoform UFD2a
additional information
AI390103
isoform CHIP mutants lacking the U box domain fail to exhibit polyubiquitination activity
additional information
isoform CHIP mutants lacking the U box domain fail to exhibit polyubiquitination activity
additional information
isoform CHIP mutants lacking the U box domain fail to exhibit polyubiquitination activity
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PURIFICATION (Commentary)
ORGANISM
UNIPROT
LITERATURE
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CLONED (Commentary)
ORGANISM
UNIPROT
LITERATURE
expression in HeLa cell, Escherichia coli
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APPLICATION
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
medicine
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
medicine
low UBE4B gene expression is associated with poor outcomes in patients with neuroblastoma and with worse outcomes in all patient subgroups. UBE4B protein expression is associated with neuroblastoma tumor differentiation, and decreased UBE4B protein levels are associated with high-risk features. UBE4B protein levels are also associated with levels of phosphorylated ERK
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REF.
AUTHORS
TITLE
JOURNAL
VOL.
PAGES
YEAR
ORGANISM (UNIPROT)
PUBMED ID
SOURCE
Chatterjee, A.; Upadhyay, S.; Chang, X.; Nagpal, J.K.; Trink, B.; Sidransky, D.
U-box-type ubiquitin E4 ligase, UFD2a attenuates cisplatin mediated degradation of DELTANp63alpha
Cell Cycle
7
1231-1237
2008
Homo sapiens (O95155)
brenda
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
brenda
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)
brenda
Metzger, M.B.; Weissman, A.M.;
Working on a chain: E3s ganging up for ubiquitylation
Nat. Cell Biol.
12
1124-1126
2010
Saccharomyces cerevisiae
brenda
Huang, Y.; Minaker, S.; Roth, C.; Huang, S.; Hieter, P.; Lipka, V.; Wiermer, M.; Li, X.
An E4 ligase facilitates polyubiquitination of plant immune receptor resistance proteins in Arabidopsis
Plant Cell
26
485-496
2014
Arabidopsis thaliana
brenda
Hatakeyama, S.; Nakayama, K.I.
U-box proteins as a new family of ubiquitin ligases
Biochem. Biophys. Res. Commun.
302
635-645
2003
Mus musculus (AI390103), Mus musculus (Q9ES00), Mus musculus (Q9WUD1), Homo sapiens (HSU37219), Homo sapiens (XM006045)
brenda
Shi, D.; Pop, M.S.; Kulikov, R.; Love, I.M.; Kung, A.L.; Kung, A.; Grossman, S.R.
CBP and p300 are cytoplasmic E4 polyubiquitin ligases for p53
Proc. Natl. Acad. Sci. USA
106
16275-16280
2009
Homo sapiens
brenda
Woodfield, S.E.; Guo, R.J.; Liu, Y.; Major, A.M.; Hollingsworth, E.F.; Indiviglio, S.; Whittle, S.B.; Mo, Q.; Bean, A.J.; Ittmann, M.; Lopez-Terrada, D.; Zage, P.E.
Neuroblastoma patient outcomes, tumor differentiation, and ERK activation are correlated with expression levels of the ubiquitin ligase UBE4B
Genes Cancer
7
13-26
2016
Homo sapiens (O95155)
brenda
McDowell, M.A.; Byrne, A.M.; Mylona, E.; Johnson, R.; Sagfors, A.; Crepin, V.F.; Lea, S.; Frankel, G.
The S. Typhi effector StoD is an E3/E4 ubiquitin ligase which binds K48- and K63-linked diubiquitin
Life Sci. Alliance
2
e2018000272
2019
Salmonella enterica subsp. enterica serovar Typhi (Q8Z7T2)
brenda
Baranes-Bachar, K.; Levy-Barda, A.; Oehler, J.; Reid, D.A.; Soria-Bretones, I.; Voss, T.C.; Chung, D.; Park, Y.; Liu, C.; Yoon, J.B.; Li, W.; Dellaire, G.; Misteli, T.; Huertas, P.; Rothenberg, E.; Ramadan, K.; Ziv, Y.; Shiloh, Y.
The ubiquitin E3/E4 ligase UBE4A adjusts protein ubiquitylation and accumulation at sites of DNA damage, facilitating double-strand break repair
Mol. Cell
69
866-878.e7
2018
Homo sapiens (Q14139)
brenda
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)
brenda
Ackermann, L.; Schell, M.; Pokrzywa, W.; Kevei, E.; Gartner, A.; Schumacher, B.; Hoppe, T.
E4 ligase-specific ubiquitination hubs coordinate DNA double-strand-break repair and apoptosis
Nat. Struct. Mol. Biol.
23
995-1002
2016
Caenorhabditis elegans (Q09349), Caenorhabditis elegans
brenda
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Release 2023.1 (January 2023)
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