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Information on EC 6.2.1.45 - E1 ubiquitin-activating enzyme and Organism(s) Homo sapiens

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EC Tree
     6 Ligases
         6.2 Forming carbon-sulfur bonds
             6.2.1 Acid-thiol ligases
                6.2.1.45 E1 ubiquitin-activating enzyme
IUBMB Comments
Catalyses the ATP-dependent activation of ubiquitin through the formation of a thioester bond between the C-terminal glycine of ubiquitin and the sulfhydryl side group of a cysteine residue in the E1 protein. The two-step reaction consists of the ATP-dependent formation of an E1-ubiquitin adenylate intermediate in which the C-terminal glycine of ubiquitin is bound to AMP via an acyl-phosphate linkage, then followed by the conversion to an E1-ubiquitin thioester bond via the cysteine residue on E1 in the second step.
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Homo sapiens
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Word Map
The taxonomic range for the selected organisms is: Homo sapiens
The enzyme appears in selected viruses and cellular organisms
Reaction Schemes
+
+
[E1 ubiquitin-activating enzyme]-L-cysteine
=
+
+
S-ubiquitinyl-[E1 ubiquitin-activating enzyme]-L-cysteine
Synonyms
ubiquitin-conjugating enzyme, ube1l, ubiquitin-activating enzyme, ubiquitin-activating enzyme e1, ubiquitin-activating enzyme (e1), ubiquitin activating enzyme, sumo e1, e1 ubiquitin-activating enzyme, ubiquitin e1, ubiquitin activating enzyme e1, more
SYNONYM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
E1 ubiquitin-activating enzyme
-
-
HsUba1a
-
-
non-canonical ubiquitin activating enzyme
-
SUMO E1
-
-
UB activating enzyme
-
Uba1a
-
-
UBE1DC1A
isoform
UBE1DC1B
isoform
ubiquitin activating enzyme
-
-
ubiquitin activating enzyme E1
-
ubiquitin E1
-
-
Ubiquitin-activating enzyme
ubiquitin-activating enzyme 1
-
-
ubiquitin-activating enzyme 5
-
ubiquitin-activating enzyme 6
-
ubiquitin-activating enzyme E1
ubiquitin-activating enzyme E1 domain-containing protein 1
-
ubiquitin-activating enzyme E1-domain containing 1
-
ubiquitin-activating enzyme, UBE1
-
-
ubiquitin-like modifier-activating enzyme 1
-
ubiquitin-like modifier-activating enzyme 5
-
ubiquitin-like modifier-activating enzyme 6
-
REACTION
REACTION DIAGRAM
COMMENTARY hide
ORGANISM
UNIPROT
LITERATURE
ATP + ubiquitin + [E1 ubiquitin-activating enzyme]-L-cysteine = AMP + diphosphate + S-ubiquitinyl-[E1 ubiquitin-activating enzyme]-L-cysteine
show the reaction diagram
PATHWAY SOURCE
PATHWAYS
-
-
SYSTEMATIC NAME
IUBMB Comments
ubiquitin:[E1 ubiquitin-activating enzyme] ligase (AMP-forming)
Catalyses the ATP-dependent activation of ubiquitin through the formation of a thioester bond between the C-terminal glycine of ubiquitin and the sulfhydryl side group of a cysteine residue in the E1 protein. The two-step reaction consists of the ATP-dependent formation of an E1-ubiquitin adenylate intermediate in which the C-terminal glycine of ubiquitin is bound to AMP via an acyl-phosphate linkage, then followed by the conversion to an E1-ubiquitin thioester bond via the cysteine residue on E1 in the second step.
SUBSTRATE
PRODUCT                       
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate) hide
LITERATURE
(Substrate)
COMMENTARY
(Product) hide
LITERATURE
(Product)
Reversibility
r=reversible
ir=irreversible
?=not specified
ATP + Oregon Green-labeled ubiquitin + [ubiquitin-activating protein E1]-L-cysteine
AMP + diphosphate + [ubiquitin-activating protein E1]-S-(Oregon Green-labeled ubiquitinyl)-L-cysteine
show the reaction diagram
-
enzyme efficiently accepts ubiquitin substrate fluorescently labeled by Oregon Green
-
-
?
ATP + SUMO2 + [ubiquitin-activating protein UBA5]-L-cysteine
AMP + diphosphate + [ubiquitin-activating protein UBA5]-S-SUMO2-L-cysteine
show the reaction diagram
SUMO2, small ubiquitin-like modifier2, an ubiquitin-like protein
enzyme greatly activates SUMO2 in the nucleus or transfers activated SUMO2 to the nucleus after it conjugated SUMO2 in the cytoplasm
-
?
ATP + ubiquitin + SUMO2
?
show the reaction diagram
UBE1DC1 greatly activates SUMO2 in the nucleus or transfers activated-SUMO2 to nucleus after conjugation of SUMO2 in the cytoplasm
-
-
?
ATP + ubiquitin + ubiquitin carrier protein E2
AMP + diphosphate + ubiquitin-(ubiquitin carrier protein E2)
show the reaction diagram
-
-
-
-
?
ATP + ubiquitin + ubiquitin-fold modifier 1
?
show the reaction diagram
-
-
-
?
ATP + ubiquitin + Ufm1
?
show the reaction diagram
-
-
-
?
ATP + ubiquitin + [6His-ubiquitin-activating enzyme E1]W-8His-Strep-HA
AMP + diphosphate + [6His-ubiquitin-activating enzyme E1]W-8His-Strep-HA-ubiquitinyl-L-cysteine
show the reaction diagram
Strep, i.e.WSHPQFEK, HA, i.e. YPYDVPDYAS, under non-reducing conditions, the intermediate complex of the thioester formation is not observed without ATP
-
-
?
ATP + ubiquitin + [E1 ubiquitin-activating enzyme]-L-cysteine
AMP + diphosphate + S-ubiquitinyl-[E1 ubiquitin-activating enzyme]-L-cysteine
show the reaction diagram
ATP + ubiquitin + [ubiquitin-activating enzyme Uba5]-L-cysteine
AMP + diphosphate + [ubiquitin-activating enzyme Uba5]-S-ubiquitinyl-L-cysteine
show the reaction diagram
the catalytic cysteine residue of isoform Uba5 is part of the adenylation domain in a alpha-helical motif
-
-
?
ATP + ubiquitin + [ubiquitin-activating protein E1]-L-cysteine
AMP + diphosphate + [ubiquitin-activating protein E1]-S-ubiquitinyl-L-cysteine
show the reaction diagram
-
-
-
-
?
ATP + ubiquitin + [ubiquitin-activating protein Uba1a]-L-cysteine
AMP + diphosphate + [ubiquitin-activating protein Uba1a]-S-ubiquitinyl-L-cysteine
show the reaction diagram
-
-
-
-
?
ATP + ubiquitin + [ubiquitin-activating protein Uba6]-L-cysteine
AMP + diphosphate + [ubiquitin-activating protein Uba6]-S-ubiquitinyl-L-cysteine
show the reaction diagram
isoform Uba6 forms a covalent link with ubiquitin in vitro and in vivo, which is sensitive to reducing conditions. Recombinant E1 enzyme Uba6 can activate ubiquitin and transfer it onto the ubiquitin-conjugating enzyme UbcH5B. Ubiquitin activated by Uba6 can be used for ubiquitylation of p53 and supports the autoubiquitylation of the E3 ubiquitin ligases HectH9 and E6-AP
-
-
?
ATP + ubiquitin + [ubiquitin-activating protein UBE1]-L-cysteine
AMP + diphosphate + [ubiquitin-activating protein UBE1]-S-ubiquitinyl-L-cysteine
show the reaction diagram
-
-
-
?
ATP + ubiquitin fold modifier1 + [ubiquitin-activating enzyme Uba5]-L-cysteine
AMP + diphosphate + [ubiquitin-activating enzyme Uba5]-S-(ubiquitin fold modifier1)-L-cysteine
show the reaction diagram
the catalytic cysteine residue of isoform Uba5 is part of the adenylation domain in a alpha-helical motif
-
-
?
ATP + Ufm1 + [ubiquitin-activating protein UBA5]-L-cysteine
AMP + diphosphate + [ubiquitin-activating protein UBA5]-S-Ufm1-L-cysteine
show the reaction diagram
Ufm1, ubiquitin-fold modifier 1, an ubiquitin-like protein
-
-
?
additional information
?
-
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
ATP + ubiquitin + [E1 ubiquitin-activating enzyme]-L-cysteine
AMP + diphosphate + S-ubiquitinyl-[E1 ubiquitin-activating enzyme]-L-cysteine
show the reaction diagram
additional information
?
-
COFACTOR
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
METALS and IONS
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
Zinc
isoform UBA5 maintains a zinc-binding site that is coordinated by four cysteines with tetrahedral geometry
INHIBITOR
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
(3E)-4-[(5R,8S)-5-methyl-6,9,13-trioxo-8-(propan-2-yl)-10-oxa-3,17-dithia-7,14,19,20-tetraazatricyclo[14.2.1.1~2,5~]icosa-1(18),2(20),16(19)-trien-11-yl]but-3-en-1-yl octanoate
-
-
(5R,8S)-11-ethenyl-5-methyl-8-(propan-2-yl)-10-oxa-3,17-dithia-7,14,19,20-tetraazatricyclo[14.2.1.1~2,5~]icosa-1(18),2(20),16(19)-triene-6,9,13-trione
-
-
(5R,8S)-5-methyl-11-[(1E)-6-oxotridec-1-en-1-yl]-8-(propan-2-yl)-10-oxa-3,17-dithia-7,14,19,20-tetraazatricyclo[14.2.1.1~2,5~]icosa-1(18),2(20),16(19)-triene-6,9,13-trione
-
-
(5R,8S)-5-methyl-8-(propan-2-yl)-11-[(1E)-4-sulfanylbut-1-en-1-yl]-10-oxa-3,17-dithia-7,14,19,20-tetraazatricyclo[14.2.1.1~2,5~]icosa-1(18),2(20),16(19)-triene-6,9,13-trione
-
-
1-(3-chloro-4-fluorophenyl)-4-[(5-nitro-2-furyl)methylene]-3,5-pyrazolidinedione
-
i.e. PYZD-4409, small molecule inhibitor. PYZD-4409 induces cell death in malignant cells and preferentially inhibits the clonogenic growth of primary acute myeloid leukemia cells compared with normal hematopoietic cells
4[4-(5-nitro-furan-2-ylmethylene)-3,5-dioxo-pyrazolidin-1-yl]-benzoic acid ethyl ester
ginsenoside Re
-
inhibits ubiquitin-activating enzyme, from Panax ginseng roots, a traditional herbal medicine or food
ginsenoside Rg1
-
inhibit ubiquitin-activating enzyme, from Panax ginseng roots, a traditional herbal medicine or food, causes 89.2% inhibition at 0.05 mM
largazole
-
largazole and its ester and ketone analogues selectively inhibit human UBA1 enzyme and inhibit ubiquitin conjugation to cyclin-dependent kinase inhibitor p27Kip1 and TRF1 in vitro, mechanism of E1 inhibition, overview. Largazole and its derivatives specifically inhibit the adenylation step of the E1 reaction while having no effect on thioester bond formation between ubiquitin and E1. Upon incubation with E1, largazole or largazole ester reduce the amount of ubiquitin molecules that are transferred from E1 to E2 in a dose-dependent fashion. E1 inhibition appears to be specific to human E1. Largazole analogues do not significantly inhibit SUMO E1
LMO2
interaction between LMO2 and UBA6 blocks the recruitment of USE1 by UBA6 in a dose-dependent manner.. The LMO2 protein interacts with the E1 ubiquitin-activating enzyme UBA6 at the C-terminal ubiquitin fold domain (UFD), which mediates the recognition and recruitment of the E2-conjugating enzyme USE1. The LMO2-UBA6 interaction leads to the decline of the overall cellular FAT10ylation level as well as the FAT10ylation and degradation of a known FAT10 substrate p62. Interaction analysis of LMO2 with isolated UBA6 domains, LMO2 interacts with UBA6 at the ubiquitin-fold domain, overview. LMO2 co-localizes with UBA6 and USE1 primarily in the cytoplasm of epithelium-derived cells
-
PYR-41
an Uba1 inhibitor
S-[(3E)-5-hydroxy-7-({[(4R)-4-{[(3S)-2-methoxy-4-methylpent-1-en-3-yl]carbamoyl}-4-methyl[4,5-dihydro[2,4'-bi-1,3-thiazole]]-2'-yl]methyl}amino)-7-oxohept-3-en-1-yl] octanethioate
-
-
[ubiquitin carrier protein Ubc4]-L-cysteine
-
-
-
ACTIVATING COMPOUND
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
ginsenoside Rb1
-
increases ubiquitination on E1 enzyme, from Panax ginseng roots, a traditional herbal medicine or food
ginsenoside Rb2
-
increases ubiquitination on E1 enzyme, from Panax ginseng roots, a traditional herbal medicine or food
ginsenoside Rc
-
increases ubiquitination on E1 enzyme, from Panax ginseng roots, a traditional herbal medicine or food
ginsenoside Rd
-
increases ubiquitination on E1 enzyme, from Panax ginseng roots, a traditional herbal medicine or food
KM VALUE [mM]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
0.0047 - 0.208
ATP
0.00017
Oregon Green-labeled ubiquitin
-
pH 7.5, 25°C
-
0.00017 - 0.029
ubiquitin
0.000073 - 0.000135
ubiquitin carrier protein E2
TURNOVER NUMBER [1/s]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
0.005 - 6
ATP
0.005 - 6
ubiquitin
0.005 - 6
ubiquitin carrier protein E2
Ki VALUE [mM]
INHIBITOR
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
0.0035
[ubiquitin carrier protein Ubc4]-L-cysteine
-
pH 7.5, 25°C
-
IC50 VALUE [mM]
INHIBITOR
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
0.0628
ginsenoside Re
Homo sapiens
-
recombinant enzyme, pH 7.6, 37°C
0.0035
ginsenoside Rg1
Homo sapiens
-
recombinant enzyme, pH 7.6, 37°C
additional information
4[4-(5-nitro-furan-2-ylmethylene)-3,5-dioxo-pyrazolidin-1-yl]-benzoic acid ethyl ester
Homo sapiens
-
inhibitor blocks loading of immobilized His6-tagged E1 with ubiquitin with an IC50 below 10 microM
pH OPTIMUM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
7.6
-
assay at
TEMPERATURE OPTIMUM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
30
-
assay at
ORGANISM
COMMENTARY hide
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
SOURCE TISSUE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
SOURCE
fetal brain
Manually annotated by BRENDA team
embryonic kidney
Manually annotated by BRENDA team
colon carcinoma cell
Manually annotated by BRENDA team
additional information
LOCALIZATION
ORGANISM
UNIPROT
COMMENTARY hide
GeneOntology No.
LITERATURE
SOURCE
GENERAL INFORMATION
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
malfunction
metabolism
physiological function
additional information
UNIPROT
ENTRY NAME
ORGANISM
NO. OF AA
NO. OF TRANSM. HELICES
MOLECULAR WEIGHT[Da]
SOURCE
SEQUENCE
LOCALIZATION PREDICTION?
UBA6_HUMAN
1052
0
117970
Swiss-Prot
other Location (Reliability: 1)
UBA1_HUMAN
1058
0
117849
Swiss-Prot
other Location (Reliability: 5)
A0A024R1A3_HUMAN
1058
0
117849
TrEMBL
other Location (Reliability: 5)
Q712V1_HUMAN
38
0
4486
TrEMBL
-
UBA5_HUMAN
404
0
44863
Swiss-Prot
-
MOLECULAR WEIGHT
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
110450
x * 110450, calculated
112000
-
analytical ultracentrifugation
117000
x * 117000, SDS-PAGE
117300
-
1 * 117300, calculated
118000
SDS-PAGE
42000
-
x * 42000, recombinant mRFP-enzyme, SDS-PAGE
SUBUNIT
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
dimer
homodimer
dimerization of UBA5 is required for UFM1 activation. The active site Cys of UBA5 (Cys 250) is located within the adenylation domain
monomer
additional information
POSTTRANSLATIONAL MODIFICATION
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
additional information
-
conjugation of the ubiquitin activating enzyme UBE1 with the ubiquitin-like modifier FAT10 targets it for proteasomal degradation
CRYSTALLIZATION (Commentary)
ORGANISM
UNIPROT
LITERATURE
enzyme exists in two splice variants. To obtain high resolution crystals of UBA5, the N-terminal region of the long isoform, residues 1–56, are deleted and residues 330–404 of the C-terminal domain are also removed. The removal of the CTD thus does not abrogate formation of the UBA5-UFM1 thioester intermediate. Crystals to 2.0 A resolution, and molecular replacement based on PDB structure 1ZFN. Structure shows similarities to both E1 and E1-like enzymes and is composed of an ATP-binding domain that consists of an eight-stranded beta-sheet surrounded by seven alpha-helices. UBA5 maintains a zinc-binding site that is coordinated by four cysteines with tetrahedral geometry
molecular modelling based on the crystal structure of Saccharomyces cerevisiae E1 and Mus musculus E1 and molecular dynamics simulation in water of the human E1-Ub complex
purified recombinant N-terminal enzyme domains comprising residues 1-439, hanging drop vapor diffusion method, mixing of 0.0015 ml of 15 mg/ml protein in 10mM Tris-HCl, pH 8.0, 150mM NaCl, and 2 mM DTT, with 0.0015 ml of reservoir solution containing 0.1 M Na3-citrate, pH 5.6, and 3.2 M NH4Ac, microseeding, 3 days, 21°C, X-ray diffraction structure determination and analysis at 2.75 A resolution
purified UBA5-UFM1 complex, containing both the adenylation domain and the UIS of UBA5, X-ray diffraction structure determination and analysis at 1.85-2.10 A
to 2.0 A resolution using molecular replacement based on PDB entry 1ZFN. UBA5 structure shows similarities to both E1 and E1-like enzymes and is composed of an ATP-binding domain that consists of an eight-stranded beta-sheet surrounded by seven alpha-helices. UBA5 maintains a zinc-binding site that is coordinated by four cysteines with tetrahedral geometry
PROTEIN VARIANTS
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
C632A
-
generation of an active site cysteine mutant of HA-UBE1
D290K/C250A
in this heterodimer, the UBA5 subunit that can form the thioester bond with UFM1 is missing the UFC1 binding site. In the UBA5 (D290K)-UBA5 (K271D/C250A DELTADUIS) heterodimer, binding to the UIS and charging can only take place on the same monomer, thereby supporting a cis-binding mechanism
D576A
D576E
D576N
D616R
site-directed mutagenesis
D623R
site-directed mutagenesis
E601R
site-directed mutagenesis
H614R
site-directed mutagenesis
K528A
Q608R
site-directed mutagenesis
S621R
site-directed mutagenesis
additional information
PURIFICATION (Commentary)
ORGANISM
UNIPROT
LITERATURE
Ni-NTA column chromatography
recombinant enzyme, purification on Ni-NTA superflow sepharose and strep-tactin sepharose which is based on UB-UBE1 high-energy thioester bonded intermediate complex
recombinant FLAG-tagged wild-type and mutant enzmyes from Escherichia coli strain BL21 by affinity chromatography
recombinant GST-tagged enzyme from Hi5 insect cells by glutathione affinity chromatography, tag cleavage by thrombin, and gel filtration
-
recombinant His-tagged N-terminal enzyme domains from Escherichia coli strain BL21(DE3) by nickel affinity chromatography, anion exchange chromatography, tag cleavage by 3C protease, another step of nickel affinity chromatography, followed by gel filtration
recombinant His-tagged wild-type and mutant enzmyes from Escherichia coli strain BL21 by nickel affinity chromatography
recombinant mRFP-enzyme from Escherichia coli strain DH5alpha by combined anion exchange/affinity chromatography and gel filtration
-
recombinant N-terminally His6-tagged enzyme UBA5 from Escherichia coli by nickel affinity chromatography
recombinant protein
recombinant protein is purified by Ni-NTA His-Bind Superflow Sepharose and Strep-Tactin Sepahrose
recombinant tagged full-length wild-type enzyme and truncated mutant versions from Escherichia coli by affinity chromatography
CLONED (Commentary)
ORGANISM
UNIPROT
LITERATURE
expressed in Escherichia coli Rosetta cells and in AD-293 cells
expression in baculoviral system
-
expression in BL-21 cell
expression in Escherichia coli
full length of human UBE1 is expressed in Escherichia coli via pET28b vector
gene Uba1, recombinant expression of His-tagged wild-type and mutant enzmyes from in Escherichia coli strain BL21, recombinant coexpression FLAG-tagged pairs of an engineered ubiquitin and engineered Uba1 or Uba6, that are generated for exclusive interactions, in HEK-293 cells from lentiviral vectors, 697 potential Uba6 targets and 527 potential Uba1 targets with 258 overlaps are identified
gene Uba6, recombinant expression of His-tagged wild-type and mutant enzmyes from in Escherichia coli strain BL21, recombinant coexpression FLAG-tagged pairs of an engineered ubiquitin and engineered Uba1 or Uba6, that are generated for exclusive interactions, in HEK-293 cells from lentiviral vectors, 697 potential Uba6 targets and 527 potential Uba1 targets with 258 overlaps are identified
HEK293 cells are transiently co-transfected with expression plasmids for HA-UBE1, the HA-tagged active site cysteine mutant UBE1 C632A, a His3-FLAG-tagged FAT10, a His3-FLAG-tagged FAT10 mutant lacking a diglycine motif at the C-terminus, or a His3-FLAG-tagged lysine-less FAT10 mutant
-
recombinant baculovirus-mediated expression of the GST-tagged enzyme in Hi5 insect cells using the pFastBacHTA vector
-
recombinant expression of mRFP-enzyme in Escherichia coli strain DH5alpha, linking of ubiquitin to the C-terminus of RFP through a peptide bond
-
recombinant expression of N-terminally His6-tagged enzyme UBA5 in Escherichia coli
recombinant expression of N-terminally His6-tagged N-terminal domains of the enzyme, residues 1-439, in Escherichia coli strain BL21(DE3) from vector pETDuet-1
recombinant transient overexpression of GST-tagged or Myc-tagged full-length wild-type enzyme and truncated mutant versions in HEK-293T cells, recombinant expression of UBA6 from pGEX-4T-1/pGEX4T-1-UBA6/pGEX4T-1-UFD plasmids in Escherichia coli
APPLICATION
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
drug development
the ubiquitin-activating enzyme E1 is a therapeutic target for the treatment of restenosis
medicine
synthesis
expression of the full length of human UBE1 in Escherichia coli and purification by Ni-NTA superflow sepharose and strep-tactin sepharose which is based on UB-UBE1 high-energy thioester bonded intermediate complex. Purified UBE1 can activate and conjugate UB to ubiquitin-conjugating enzyme E2s
REF.
AUTHORS
TITLE
JOURNAL
VOL.
PAGES
YEAR
ORGANISM (UNIPROT)
PUBMED ID
SOURCE
Handley, P.M.; Mueckler, M.; Siegel, N.R.; Ciechanover, A.; Schwartz, A.I.
Molecular cloning, sequence, and tissue distribution of the human ubiquitin-activating enzyme E1
Proc. Natl. Acad. Sci. USA
88
258-262
1991
Homo sapiens (P22314), Homo sapiens
Manually annotated by BRENDA team
Yang, Y.; Kitagaki, J.; Dai, R.M.; Tsai, Y.C.; Lorick, K.L.; Ludwig, R.L.; Pierre, S.A.; Jensen, J.P.; Davydov, I.V.; Oberoi, P.; Li, C.C.; Kenten, J.H.; Beutler, J.A.; Vousden, K.H.; Weissman, A.M.
Inhibitors of ubiquitin-activating enzyme (E1), a new class of potential cancer therapeutics
Cancer Res.
67
9472-9481
2007
Homo sapiens, Mus musculus
Manually annotated by BRENDA team
Tokgoez, Z.; Bohnsack, R.N.; Haas, A.L.
Pleiotropic effects of ATP*Mg2+ binding in the catalytic cycle of ubiquitin-activating enzyme
J. Biol. Chem.
281
14729-14737
2006
Homo sapiens
Manually annotated by BRENDA team
Pelzer, C.; Kassner, I.; Matentzoglu, K.; Singh, R.K.; Wollscheid, H.P.; Scheffner, M.; Schmidtke, G.; Groettrup, M.
UBE1L2, a novel E1 enzyme specific for ubiquitin
J. Biol. Chem.
282
23010-23014
2007
Homo sapiens, Homo sapiens (A0AVT1), Mus musculus
Manually annotated by BRENDA team
Nouspikel, T.; Hanawalt, P.C.
Impaired nucleotide excision repair upon macrophage differentiation is corrected by E1 ubiquitin-activating enzyme
Proc. Natl. Acad. Sci. USA
103
16188-16193
2006
Homo sapiens
Manually annotated by BRENDA team
Zheng, M.; Gu, X.; Zheng, D.; Yang, Z.; Li, F.; Zhao, J.; Xie, Y.; Ji, C.; Mao, Y.
UBE1DC1, an ubiquitin-activating enzyme, activates two different ubiquitin-like proteins
J. Cell. Biochem.
104
2324-2334
2008
Homo sapiens (Q9GZZ9)
Manually annotated by BRENDA team
Xu, G.W.; Ali, M.; Wood, T.E.; Wong, D.; Maclean, N.; Wang, X.; Gronda, M.; Skrtic, M.; Li, X.; Hurren, R.; Mao, X.; Venkatesan, M.; Beheshti Zavareh, R.; Ketela, T.; Reed, J.C.; Rose, D.; Moffat, J.; Batey, R.A.; Dhe-Paganon, S.; Schimmer, A.D.
The ubiquitin-activating enzyme E1 as a therapeutic target for the treatment of leukemia and multiple myeloma
Blood
115
2251-2259
2010
Homo sapiens, Mus musculus
Manually annotated by BRENDA team
Bacik, J.P.; Walker, J.R.; Ali, M.; Schimmer, A.D.; Dhe-Paganon, S.
Crystal structure of the human ubiquitin-activating enzyme 5 (UBA5) bound to ATP: mechanistic insights into a minimalistic E1 enzyme
J. Biol. Chem.
285
20273-20280
2010
Homo sapiens (Q9GZZ9), Homo sapiens
Manually annotated by BRENDA team
Brahemi, G.; Burger, A.M.; Westwell, A.D.; Brancale, A.
Homology modelling of human E1 ubiquitin activating enzyme
Lett. Drug Des. Discov.
7
57-62
2010
Homo sapiens (P22314), Homo sapiens
Manually annotated by BRENDA team
Zheng, M.; Liu, J.; Yang, Z.; Gu, X.; Li, F.; Lou, T.; Ji, C.; Mao, Y.
Expression, purification and characterization of human ubiquitin-activating enzyme, UBE1
Mol. Biol. Rep.
37
1413-1419
2010
Homo sapiens, Homo sapiens (Q712V1)
Manually annotated by BRENDA team
Wee, K.E.; Lai, Z.; Auger, K.R.; Ma, J.; Horiuchi, K.Y.; Dowling, R.L.; Dougherty, C.S.; Corman, J.I.; Wynn, R.; Copeland, R.A.
Steady-state kinetic analysis of human ubiquitin-activating enzyme (E1) using a fluorescently labeled ubiquitin substrate
J. Protein Chem.
19
489-498
2000
Homo sapiens
Manually annotated by BRENDA team
Xie, S.T.
Expression, purification, and crystal structure of N-terminal domains of human ubiquitin-activating enzyme (E1)
Biosci. Biotechnol. Biochem.
78
1542-1549
2014
Homo sapiens (P22314), Homo sapiens
Manually annotated by BRENDA team
Chang, T.; Huang, Y.; Ou, Y.
The role of ginsenosides in inhibiting ubiquitin activating enzyme (E1) activity
J. Funct. Foods
7
462-470
2014
Homo sapiens
-
Manually annotated by BRENDA team
Bialas, J.; Groettrup, M.; Aichem, A.
Conjugation of the ubiquitin activating enzyme UBE1 with the ubiquitin-like modifier FAT10 targets it for proteasomal degradation
PLoS ONE
10
e0120329
2015
Homo sapiens
Manually annotated by BRENDA team
Ungermannova, D.; Parker, S.J.; Nasveschuk, C.G.; Wang, W.; Quade, B.; Zhang, G.; Kuchta, R.D.; Phillips, A.J.; Liu, X.
Largazole and its derivatives selectively inhibit ubiquitin activating enzyme (E1)
PLoS ONE
7
e29208
2012
Homo sapiens, Schizosaccharomyces pombe
Manually annotated by BRENDA team
Qin, Z.; Cui, B.; Jin, J.; Song, M.; Zhou, B.; Guo, H.; Qian, D.; He, Y.; Huang, L.
The ubiquitin-activating enzyme E1 as a novel therapeutic target for the treatment of restenosis
Atherosclerosis
247
142-153
2016
Homo sapiens (P22314)
Manually annotated by BRENDA team
Wu, C.; Liu, Y.; Gu, X.; Zhu, T.; Yang, S.; Sun, W.
LMO2 blocks the UBA6-USE1 interaction and downstream FAT10ylation by targeting the ubiquitin fold domain of UBA6
Biochem. Biophys. Res. Commun.
478
1442-1448
2016
Homo sapiens (A0AVT1)
Manually annotated by BRENDA team
Oweis, W.; Padala, P.; Hassouna, F.; Cohen-Kfir, E.; Gibbs, D.R.; Todd, E.A.; Berndsen, C.E.; Wiener, R.
Trans-binding mechanism of ubiquitin-like protein activation revealed by a UBA5-UFM1 complex
Cell Rep.
16
3113-3120
2016
Homo sapiens (Q9GZZ9)
Manually annotated by BRENDA team
Liu, X.; Zhao, B.; Sun, L.; Bhuripanyo, K.; Wang, Y.; Bi, Y.; Davuluri, R.; Duong, D.; Nanavati, D.; Yin, J.; Kiyokawa, H.
Orthogonal ubiquitin transfer identifies ubiquitination substrates under differential control by the two ubiquitin activating enzymes
Nat. Commun.
8
14286
2017
Homo sapiens (A0AVT1), Homo sapiens (P22314)
Manually annotated by BRENDA team
Liu, X.; Sun, L.; Gursel, D.B.; Cheng, C.; Huang, S.; Rademaker, A.W.; Khan, S.A.; Yin, J.; Kiyokawa, H.
The non-canonical ubiquitin activating enzyme UBA6 suppresses epithelial-mesenchymal transition of mammary epithelial cells
Oncotarget
8
87480-87493
2017
Homo sapiens (A0AVT1), Homo sapiens
Manually annotated by BRENDA team