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Information on EC 2.3.2.B12 - ubiquitin transferase U-box E4 and Organism(s) Homo sapiens and UniProt Accession Q14139

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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Select one or more organisms in this record: ?
This record set is specific for:
Homo sapiens
UNIPROT: Q14139 not found.
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The taxonomic range for the selected organisms is: Homo sapiens
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
CYC4
HSU37219
-
PRP19
XM006045
-
SYSTEMATIC NAME
IUBMB Comments
[U-box-E4-ubiquitin-carrier protein]-S-ubiquitinyl-L-cysteine:acceptor protein-ubiquitinyl ubiquitin transferase (isopeptide bond-forming)
-
SUBSTRATE
PRODUCT                       
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate) hide
LITERATURE
(Substrate)
COMMENTARY
(Product) hide
LITERATURE
(Product)
Reversibility
r=reversible
ir=irreversible
?=not specified
[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
-
-
?
[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
-
-
?
[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
-
-
?
[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
-
-
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
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
-
-
?
additional information
?
-
ORGANISM
COMMENTARY hide
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
isoform Ube4A, cf. EC 2.3.2.27
UniProt
Manually annotated by BRENDA team
SOURCE TISSUE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
SOURCE
HSU37219, XM006045
-
Manually annotated by BRENDA team
HSU37219, XM006045
-
Manually annotated by BRENDA team
HSU37219, XM006045
-
Manually annotated by BRENDA team
HSU37219, XM006045
-
Manually annotated by BRENDA team
HSU37219, XM006045
-
Manually annotated by BRENDA team
HSU37219, XM006045
-
Manually annotated by BRENDA team
LOCALIZATION
ORGANISM
UNIPROT
COMMENTARY hide
GeneOntology No.
LITERATURE
SOURCE
HSU37219, XM006045
-
Manually annotated by BRENDA team
GENERAL INFORMATION
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
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
UNIPROT
ENTRY NAME
ORGANISM
NO. OF AA
NO. OF TRANSM. HELICES
MOLECULAR WEIGHT[Da]
SOURCE
SEQUENCE
LOCALIZATION PREDICTION?
UBE4A_HUMAN
1066
0
122561
Swiss-Prot
-
CLONED (Commentary)
ORGANISM
UNIPROT
LITERATURE
expression in HeLa cell, Escherichia coli
HSU37219, XM006045
expression in JHU-022 cell and H-1299 cell
APPLICATION
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
medicine
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)
Manually annotated by BRENDA team
Hatakeyama, S.; Nakayama, K.I.
U-box proteins as a new family of ubiquitin ligases
Biochem. Biophys. Res. Commun.
302
635-645
2003
Homo sapiens (HSU37219), Homo sapiens (XM006045), Mus musculus (AI390103), Mus musculus (Q9ES00), Mus musculus (Q9WUD1)
Manually annotated by BRENDA team
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
Manually annotated by BRENDA team
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)
Manually annotated by BRENDA team
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)
Manually annotated by BRENDA team