Any feedback?
Please rate this page
(enzyme.php)
(0/150)

BRENDA support

BRENDA Home
show all | hide all No of entries

Information on EC 2.3.2.23 - E2 ubiquitin-conjugating enzyme and Organism(s) Homo sapiens

for references in articles please use BRENDA:EC2.3.2.23
Please wait a moment until all data is loaded. This message will disappear when all data is loaded.
EC Tree
     2 Transferases
         2.3 Acyltransferases
             2.3.2 Aminoacyltransferases
                2.3.2.23 E2 ubiquitin-conjugating enzyme
IUBMB Comments
The E2 ubiquitin-conjugating enzyme acquires the activated ubquitin from the E1 ubiquitin-activating enzyme (EC 6.2.1.45) and binds it via a transthioesterification reaction to itself. In the human enzyme the catalytic center is located at Cys-87 where ubiquitin is bound via its C-terminal glycine in a thioester linkage.
Specify your search results
Select one or more organisms in this record: ?
This record set is specific for:
Homo sapiens
Show additional data
Do not include text mining results
Include (text mining) results
Include results (AMENDA + additional results, but less precise)
Word Map
The taxonomic range for the selected organisms is: Homo sapiens
The enzyme appears in selected viruses and cellular organisms
Reaction Schemes
S-ubiquitinyl-[E1 ubiquitin-activating enzyme]-L-cysteine
+
[E2 ubiquitin-conjugating enzyme]-L-cysteine
=
[E1 ubiquitin-activating enzyme]-L-cysteine
+
S-ubiquitinyl-[E2 ubiquitin-conjugating enzyme]-L-cysteine
Synonyms
ube2c, cdc34, ubc13, ube2t, ubch10, e2 enzyme, ube2s, ubch7, e2 ubiquitin-conjugating enzyme, ube2l3, more
SYNONYM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
alpha spectrin
-
-
E2 enzyme
E2 ubiquitin conjugating enzyme
-
-
E2 ubiquitin-conjugating enzyme
E2-conjugating enzyme
-
NEDD8-activating enzyme E1 catalytic subunit
-
SUMO E2 enzyme
-
SUMO-1-conjugating enzyme Ubc9
-
-
SUMO-conjugating enzyme UBC9
-
UBA6-specific E2 enzyme 1
-
UbcH8
UbcM2
UBE2D
-
-
Ube2J1
UBE2L3
UBE2N
UBE2R1
UBE2W
-
-
ubiquitin-conjugating enzyme
ubiquitin-conjugating enzyme (E2)
-
-
ubiquitin-conjugating enzyme E2
ubiquitin-conjugating enzyme E2 B
-
ubiquitin-conjugating enzyme E2 D1
-
ubiquitin-conjugating enzyme E2 G1
-
ubiquitin-conjugating enzyme E2 Z
-
ubiquitin-conjugating enzyme E2T
-
ubiquitination enzyme
-
REACTION
REACTION DIAGRAM
COMMENTARY hide
ORGANISM
UNIPROT
LITERATURE
S-ubiquitinyl-[E1 ubiquitin-activating enzyme]-L-cysteine + [E2 ubiquitin-conjugating enzyme]-L-cysteine = [E1 ubiquitin-activating enzyme]-L-cysteine + S-ubiquitinyl-[E2 ubiquitin-conjugating enzyme]-L-cysteine
show the reaction diagram
E2 enzymes autoubiquitinate both their active sites cysteine, described for this enzyme and lysine residues
-
REACTION TYPE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
transthioesterification
-
-
PATHWAY SOURCE
PATHWAYS
-
-
SYSTEMATIC NAME
IUBMB Comments
S-ubiquitinyl-[E1 ubiquitin-activating enzyme]-L-cysteine:[E2 ubiquitin-conjugating enzyme] ubiquitinyl transferase
The E2 ubiquitin-conjugating enzyme acquires the activated ubquitin from the E1 ubiquitin-activating enzyme (EC 6.2.1.45) and binds it via a transthioesterification reaction to itself. In the human enzyme the catalytic center is located at Cys-87 where ubiquitin is bound via its C-terminal glycine in a thioester linkage.
SUBSTRATE
PRODUCT                       
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate) hide
LITERATURE
(Substrate)
COMMENTARY
(Product) hide
LITERATURE
(Product)
Reversibility
r=reversible
ir=irreversible
?=not specified
S-SUMOyl-[E1 SUMO-activating enzyme]-L-cysteine + [Ubc9]-L-cysteine
[E1 SUMO-activating enzyme]-L-cysteine + S-SUMOyl-[Ubc9]-L-cysteine
show the reaction diagram
-
isoform Ubc9 is involved as E2 enzyme both in the ubiquitin and the ubiquitin-like SUMO pathway. Ubiquitin-like proteins SUMO-1, -2, and -3 interact with the same N-terminal region of the E2 conjugating enzyme Ubc9 with similar affinities
-
?
S-ubiquitinyl-[E1 ubiquitin-activating enzyme]-L-cysteine + [E2 ubiquitin-conjugating enzyme]-L-cysteine
[E1 ubiquitin-activating enzyme]-L-cysteine + S-ubiquitinyl-[E2 ubiquitin-conjugating enzyme]-L-cysteine
show the reaction diagram
S-ubiquitinyl-[Uba1]-L-cysteine + [Ubc5a]-L-cysteine
[Uba1]-L-cysteine + S-ubiquitinyl-[Ubc5a]-L-cysteine
show the reaction diagram
-
the E1 enzyme Uba1, the E2 enzyme UbcH5a, and the E3 enzyme TRIP12 are responsible for ubiquitylation of ubiquitin mutant G76V
-
?
[ubiquitin-activating protein E1]-S-ubiquitinyl-L-cysteine + [ubiquitin carrier protein Ubc4]-L-cysteine
[ubiquitin-activating protein E1]-L-cysteine + [ubiquitin carrier protein Ubc4]-S-ubiquitinyl-L-cysteine
show the reaction diagram
binding of Ubc4 to the E1–ubiquitin covalent intermediate leads to productive catalysis of ubiquitin transfer to Ubc4 in the form of a thioester linkage. No significant ubiquitination of Ubc4 through formation of lysyl isopeptide bonds is observed
-
-
?
[ubiquitin-activating protein Uba1a]-S-ubiquitinyl-L-cysteine + [ubiquitin-carrier-protein Ubc2b]-L-cysteine
[ubiquitin-activating protein Uba1a]-L-cysteine + [ubiquitin-carrier-protein Ubc2b]-S-ubiquitinyl-L-cysteine
show the reaction diagram
-
-
-
-
?
[ubiquitin-activating protein Uba1]-S-ubiquitinyl-L-cysteine + [ubiquitin-carrier-protein Ubc2b]-L-cysteine
[ubiquitin-activating protein Uba1]-L-cysteine + [ubiquitin-carrier-protein Ubc2b]-S-ubiquitinyl-L-cysteine
show the reaction diagram
-
-
-
?
[ubiquitin-activating protein Uba3]-S-ubiquitinyl-L-cysteine + [ubiquitin-carrier-protein Ubc12]-L-cysteine
[ubiquitin-activating protein Uba3]-L-cysteine + [ubiquitin-carrier-protein Ubc12]-S-ubiquitinyl-L-cysteine
show the reaction diagram
-
-
-
?
[ubiquitin-activating protein Uba6]-S-ubiquitinyl-L-cysteine + [ubiquitin carrier protein UbcH5B]-L-cysteine
[ubiquitin-activating protein Uba]-L-cysteine + [ubiquitin carrier protein UbcH5B]-S-ubiquitinyl-L-cysteine
show the reaction diagram
-
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
-
?
[ubiquitin-activating protein UBE1]-S-ubiquitinyl-L-cysteine + [ubiquitin carrier protein E2]-L-cysteine
[ubiquitin-activating protein UBE1]-L-cysteine + [ubiquitin carrier protein E2]-S-ubiquitinyl-L-cysteine
show the reaction diagram
-
purified E1 enzyme UBE1 can activate and conjugate ubiquitin to ubiquitin-conjugating enzyme E2s. Transfer is restricted to distinct E2 isoforms UB2R2, UBE2W and UBE2NL
-
-
?
[ubiquitin-activating protein UBE1]-S-ubiquitinyl-L-cysteine + [ubiquitin carrier protein UB2R2]-L-cysteine
[ubiquitin-activating protein UBE1]-L-cysteine + [ubiquitin carrier protein UB2R2]-S-ubiquitinyl-L-cysteine
show the reaction diagram
-
purified E1 enzyme UBE1 can activate and conjugate ubiquitin to ubiquitin-conjugating enzyme E2s. Transfer is restricted to distinct E2 isoforms UB2R2, UBE2W and UBE2NL
-
-
?
[ubiquitin-activating protein UBE1]-S-ubiquitinyl-L-cysteine + [ubiquitin carrier protein UBE2NL]-L-cysteine
[ubiquitin-activating protein UBE1]-L-cysteine + [ubiquitin carrier protein UBE2NL]-S-ubiquitinyl-L-cysteine
show the reaction diagram
-
purified E1 enzyme UBE1 can activate and conjugate ubiquitin to ubiquitin-conjugating enzyme E2s. Transfer is restricted to distinct E2 isoforms UB2R2, UBE2W and UBE2NL
-
-
?
[ubiquitin-activating protein UBE1]-S-ubiquitinyl-L-cysteine + [ubiquitin carrier protein UBE2W]-L-cysteine
[ubiquitin-activating protein UBE1]-L-cysteine + [ubiquitin carrier protein UBE2W]-S-ubiquitinyl-L-cysteine
show the reaction diagram
-
purified E1 enzyme UBE1 can activate and conjugate ubiquitin to ubiquitin-conjugating enzyme E2s. Transfer is restricted to distinct E2 isoforms UB2R2, UBE2W and UBE2NL
-
-
?
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
S-ubiquitinyl-[E1 ubiquitin-activating enzyme]-L-cysteine + [E2 ubiquitin-conjugating enzyme]-L-cysteine
[E1 ubiquitin-activating enzyme]-L-cysteine + S-ubiquitinyl-[E2 ubiquitin-conjugating enzyme]-L-cysteine
show the reaction diagram
METALS and IONS
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
Mg2+
required in the E2 loading reaction
INHIBITOR
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
1-(1,3-benzothiazol-2-yl)methanamine
i.e. EM04, about 40% inhibition of FANCD2 ubiquination
2-amino-5-phenylfuran-3-carbonitrile
i.e. EM11, about 25% inhibition of FANCD2 ubiquination
3-(2-hydroxyphenyl)pyridin-2(1H)-one
-
3-methyl-3,4-dihydroquinazolin-2(1H)-one
i.e. EM09, about 15% inhibition of FANCD2 ubiquination
4-phenyl-1,3-thiazol-2-amine
i.e. EM17, about 60% inhibition of FANCD2 ubiquination
5,6-dibenzo[c,e][1,2]thiazine-5,5(6H)-dione
-
5-chloro-1,3-benzoxazole-2-thiol
-
6-chloro-1,3-benzoxazole-2-thiol
-
6-chloro-2,3,4,9-tetrahydro-1H-carbazole-1-carboxamide
i.e. EM02, almost complete inhibition of FANCD2 ubiquination
CC0651
a small-molecule inhibitor that selectively inhibits Ube2R1, the specialized E2 for SCF E3 ligases, which builds K48-linked polyUb chains on its targets for proteasomal degradation. In a co-crystal structure of Ube2R1, Ub, and CC0651, the inhibitor is sandwiched between the E2 and Ub
ethyl 3-(2,2'-dihydroxy[1,1'-biphenyl]-4-yl)propanoate
-
[1,1'-biphenyl]-2,2'-diol
-
[1,1'-biphenyl]-2-ol
-
[1,1'-biphenyl]-2-sulfonamide
-
additional information
-
ACTIVATING COMPOUND
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
additional information
-
KM VALUE [mM]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
1
S-ubiquitinyl-[E1 ubiquitin-activating enzyme]-L-cysteine
about, pH 7.5, temperature not specified in the publication
-
0.0019
[ubiquitin carrier protein Ubc4]-L-cysteine
pH 7.5, 25°C
-
0.000073 - 0.000135
[ubiquitin-carrier-protein Ubc2b]-L-cysteine
-
additional information
additional information
-
TURNOVER NUMBER [1/s]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
0.072
[ubiquitin carrier protein Ubc4]-L-cysteine
pH 7.5, 25°C
-
0.01 - 3.4
[ubiquitin-carrier-protein Ubc2b]-L-cysteine
-
IC50 VALUE [mM]
INHIBITOR
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
20
3-(2-hydroxyphenyl)pyridin-2(1H)-one
Homo sapiens
above, pH and temperature not specified in the publication
3
5,6-dibenzo[c,e][1,2]thiazine-5,5(6H)-dione
Homo sapiens
above, pH and temperature not specified in the publication
3
6-chloro-1,3-benzoxazole-2-thiol
Homo sapiens
above, pH and temperature not specified in the publication
3
ethyl 3-(2,2'-dihydroxy[1,1'-biphenyl]-4-yl)propanoate
Homo sapiens
pH and temperature not specified in the publication
5.8
[1,1'-biphenyl]-2,2'-diol
Homo sapiens
pH and temperature not specified in the publication
1.9
[1,1'-biphenyl]-2-ol
Homo sapiens
pH and temperature not specified in the publication
3.1
[1,1'-biphenyl]-2-sulfonamide
Homo sapiens
pH and temperature not specified in the publication
pH OPTIMUM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
TEMPERATURE OPTIMUM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
20
assay at
32
assay at
ORGANISM
COMMENTARY hide
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
SOURCE TISSUE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
SOURCE
Ube2T is overexpressed in several cancers
Manually annotated by BRENDA team
quantitative real-time PCR enzyme expression analysis in gastric cancer cell lines, overview
Manually annotated by BRENDA team
colon carcinoma cell
Manually annotated by BRENDA team
most abundant expression
Manually annotated by BRENDA team
additional information
-
most E2 enzymes have been identified in a wide variety of tissues and cell types
Manually annotated by BRENDA team
LOCALIZATION
ORGANISM
UNIPROT
COMMENTARY hide
GeneOntology No.
LITERATURE
SOURCE
additional information
GENERAL INFORMATION
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
evolution
malfunction
metabolism
physiological function
additional information
UNIPROT
ENTRY NAME
ORGANISM
NO. OF AA
NO. OF TRANSM. HELICES
MOLECULAR WEIGHT[Da]
SOURCE
SEQUENCE
LOCALIZATION PREDICTION?
UB2E1_HUMAN
193
0
21404
Swiss-Prot
other Location (Reliability: 1)
UB2E2_HUMAN
201
0
22255
Swiss-Prot
other Location (Reliability: 1)
UB2E3_HUMAN
207
0
22913
Swiss-Prot
other Location (Reliability: 2)
UB2G1_HUMAN
170
0
19509
Swiss-Prot
other Location (Reliability: 1)
UB2G2_HUMAN
165
0
18566
Swiss-Prot
other Location (Reliability: 2)
UB2J1_HUMAN
318
1
35199
Swiss-Prot
other Location (Reliability: 2)
UBE2S_HUMAN
222
0
23845
Swiss-Prot
other Location (Reliability: 2)
UBE2T_HUMAN
197
0
22521
Swiss-Prot
other Location (Reliability: 4)
UBE2U_HUMAN
321
0
37741
Swiss-Prot
other Location (Reliability: 2)
UBE2W_HUMAN
151
0
17331
Swiss-Prot
other Location (Reliability: 2)
UBE2Z_HUMAN
354
0
38210
Swiss-Prot
other Location (Reliability: 2)
UBE2H_HUMAN
183
0
20655
Swiss-Prot
other Location (Reliability: 3)
UBE2K_HUMAN
200
0
22407
Swiss-Prot
other Location (Reliability: 2)
UBE2N_HUMAN
152
0
17138
Swiss-Prot
other Location (Reliability: 4)
UB2J2_HUMAN
259
1
28898
Swiss-Prot
other Location (Reliability: 5)
UB2L3_HUMAN
154
0
17862
Swiss-Prot
other Location (Reliability: 2)
UB2L5_HUMAN
154
0
17875
Swiss-Prot
other Location (Reliability: 2)
UB2L6_HUMAN
153
0
17769
Swiss-Prot
other Location (Reliability: 2)
UB2Q1_HUMAN
422
0
46127
Swiss-Prot
other Location (Reliability: 2)
UB2Q2_HUMAN
375
0
42818
Swiss-Prot
other Location (Reliability: 3)
UBE2A_HUMAN
152
0
17315
Swiss-Prot
Mitochondrion (Reliability: 5)
UBE2B_HUMAN
152
0
17312
Swiss-Prot
other Location (Reliability: 5)
UBE2C_HUMAN
179
0
19652
Swiss-Prot
other Location (Reliability: 4)
U2QL1_HUMAN
161
0
18338
Swiss-Prot
other Location (Reliability: 1)
UB2D1_HUMAN
147
0
16602
Swiss-Prot
other Location (Reliability: 3)
UB2D2_HUMAN
147
0
16735
Swiss-Prot
other Location (Reliability: 2)
UB2D3_HUMAN
147
0
16687
Swiss-Prot
other Location (Reliability: 2)
UB2D4_HUMAN
147
0
16649
Swiss-Prot
other Location (Reliability: 2)
UB2R1_HUMAN
236
0
26737
Swiss-Prot
other Location (Reliability: 3)
UB2R2_HUMAN
238
0
27166
Swiss-Prot
other Location (Reliability: 2)
UBA1_HUMAN
1058
0
117849
Swiss-Prot
-
UBC9_HUMAN
158
0
18007
Swiss-Prot
Secretory Pathway (Reliability: 1)
UB2V1_HUMAN
147
0
16495
Swiss-Prot
-
UB2V2_HUMAN
145
0
16363
Swiss-Prot
-
UE2NL_HUMAN
153
0
17377
Swiss-Prot
-
UBA3_HUMAN
463
0
51852
Swiss-Prot
-
PDB
SCOP
CATH
UNIPROT
ORGANISM
SUBUNIT
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
dimer
-
E2 enzymes spontaneously dimerize in solution, in vitro, in absence of charged ubiquitin
additional information
POSTTRANSLATIONAL MODIFICATION
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
sumoylation
CRYSTALLIZATION (Commentary)
ORGANISM
UNIPROT
LITERATURE
crystal structure of an E2-Ub oxyester conjugate (Ube2D2) in a closed state showing the interface formed between the E2 crossover helix and the I44 surface of Ub upon binding a RING E3 (BIRC7, PDB ID 4AUQ)
purified recombinant detagged UBE2Z, microcrystals are grown by mixing of 12 mg/ml protein solution with crystallization solution containing 25% w/v PEG 6000 and 0.1 M Tris, pH 8.0, a seed stock is generated from these microcrystals and used in cross-seeding, diffraction quality crystals grow at room temperature in 8-25% w/v PEG 1500, 0.1 M D-malic acid-MES-TRIS buffer at pH 5.0-7.5, X-ray diffraction structure determination and analysis at 2.1 A resolution, molecular replacement using the structure of UBE2D3 (PDB ID 1X23) as the search model for UBE2Z. The determined structure lacks the N-terminal 98 residues of the protein corresponding to the UBE2Z N-terminal extension
Ube2T in complex with inhibitor 1-(1,3-benzothiazol-2-yl)methanamine, X-ray diffraction crystal structure analysis, PDB ID 5NGZ
PROTEIN VARIANTS
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
A157C
a naturally occuring mutation involved in the Fanconi anaemia syndrome
C136F
-
mutation results in constitutive binding of UbcM2 to transcription factor Nrf2 and an increased half-life of the transcription factor in vivo
C93S
-
sumoylatzion-defective mutant
C94S
site-directed mutagenesis, a catalytically inactive mutant
D102K
site-directed mutagenesis, analysis of ubiquitin specificity and reaction kinetics compared to wild-type
D103K
site-directed mutagenesis, analysis of ubiquitin specificity and reaction kinetics compared to wild-type
D127G
site-directed mutagenesis
D143A
site-directed mutagenesis, analysis of ubiquitin specificity and reaction kinetics compared to wild-type
D143K
site-directed mutagenesis, analysis of ubiquitin specificity and reaction kinetics compared to wild-type
D143R
site-directed mutagenesis, analysis of ubiquitin specificity and reaction kinetics compared to wild-type
D91K
site-directed mutagenesis, analysis of ubiquitin specificity and reaction kinetics compared to wild-type
DELTA946
truncation of the Uba3 carboxyl-terminal beta-grasp domain, no effect on cognate Ubc12 thiolester formation
K323R
mutation in site of auto-FAT10ylation. Mutation does not abolish auto-FAT10ylation of USE1, but every other lysine can instead be modified with FAT10
K86V
during transfer of ubiquitin to the final substrate or E3 ligase, reaction of EC 2.3.2.27, mutant shows increased polyubiquitin chain building activity with ubiquitin mutant K48R
N80Q
during transfer of ubiquitin to the final substrate or E3 ligase, reaction of EC 2.3.2.27, mutant shows increased polyubiquitin chain building activity with ubiquitin mutant K48R
P79A
during transfer of ubiquitin to the final substrate or E3 ligase, reaction of EC 2.3.2.27, mutant shows a much reduced capacity to ubiquitylate RING-E3 enzyme RNF25
Q126A
site-directed mutagenesis
Q126G
site-directed mutagenesis
Q126I
site-directed mutagenesis
Q126L
site-directed mutagenesis
Q126V
site-directed mutagenesis
Q2E
a naturally occuring mutation involved in the Fanconi anaemia syndrome
Q37R
a naturally occuring mutation involved in the Fanconi anaemia syndrome
R13A/K14A
mutations in Ubc9 disrupt the interaction with SUMO-1 but do not completely abolish the interaction with E1 enzyme. Mutant displays a significantly reduced efficiency in the transfer of SUMO-1 from E1 to Ubc9, its ability to recognize substrate and transfer SUMO-1 from Ubc9 to the target protein is unaffected
R17A/K18A
mutations in Ubc9 disrupt the interaction with SUMO-1 but do not completely abolish the interaction with E1 enzyme. Mutant displays a significantly reduced efficiency in the transfer of SUMO-1 from E1 to Ubc9, its ability to recognize substrate and transfer SUMO-1 from Ubc9 to the target protein is unaffected
R94Q/L98M
during transfer of ubiquitin to the final substrate or E3 ligase, reaction of EC 2.3.2.27, mutant shows increased polyubiquitin chain building activity with ubiquitin mutant K48R
additional information
PURIFICATION (Commentary)
ORGANISM
UNIPROT
LITERATURE
recombinant GST- or His6-tagged enzyme UBE2R1 from Escherichia coli strain Rosetta (DE3) by glutathione or nickel affinity chromatography, respectively, followed by tag cleavage through TEV protease, and gel filtration
recombinant His-tagged enzyme from Escherichia coli strain BL21 (DE3) Codon Plus by nickel affinity chromatography
recombinant His-tagged wild-type and mutant enzymes from Escherichia coli by nickel affinity chromatography, followed by tag cleavage by TEV protease, dialysis, and gel filtration
recombinant His6-tagged enzyme UBE2Z from Escherichia coli strain BL21(DE3) by metal affinity chromatography, dialysis, tag cleavage through HRV 3C protease, followed by anion exchange chromatography and dialysis, gel filtration and ultrafiltration
recombinant protein, Ni-NTA column
-
CLONED (Commentary)
ORGANISM
UNIPROT
LITERATURE
expressed and transformed into Escherichia coli (BL-21 DE3) using pET22 vector in frame to a C-terminal His6 tag
-
expressed in HEK-293T, HeLa, or U2OS cells
-
expression in baculoviral system
expression in Escherichia coli
gene cdc34, recombinant His-tagged enzyme expression in Escherichia coli strain BL21 (DE3) Codon Plus
gene rad6a, the S-Flag-biotin (SFB)-tagged full length E2 is expressed in HEK-293T, HeLa, or U2OS cells, recombinant coexpression of Rad6b with E3 ubiquitin ligases RNF168 and RAD18 in E2-deficient MEF cells leading to formation of ionizing radiation-induced foci (IRIF)
gene rad6b, the S-Flag-biotin (SFB)-tagged full length E2 is expressed in HEK-293T, HeLa, or U2OS cells, recombinant coexpression of Rad6b with E3 ubiquitin ligases RNF168 and RAD18 in E2-deficient MEF cells leading to formation of ionizing radiation-induced foci (IRIF)
gene UBE2K, recombinant expression of His-tagged wild-type and mutant enzymes in Escherichia coli
gene UBE2R1 or CDC34, recombinant expression of GST- or His6-tagged enzyme in Escherichia coli strain Rosetta (DE3)
gene UBE2T, genotyping
gene UBE2T, located in chromosome 1q32.1, quantitative real-time PCR enzyme expression analysis
gene UBE2Z, sequence comparisons, recombinant overexpression of His6-tagged enzyme in Escherichia coli strain BL21(DE3)
EXPRESSION
ORGANISM
UNIPROT
LITERATURE
the majority of E2s are expressed ubiquitously
-
Ube2L3 undergoes transcriptional regulation in response to aryl hydrocarbon receptor (AHR) signaling. The resulting increase in Ube2L3 levels leads to degradation of cell cycle control proteins, identifying a connection between AHR signaling and the previously established role that Ube2L3 plays in cell cycle regulation
APPLICATION
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
diagnostics
ubiquitin-conjugating enzyme E2T is an independent prognostic factor and promotes gastric cancer progression
drug development
enzyme Ube2T represents an attractive target for the development of inhibitors. Modulation of DNA repair pathways is a strategy for the development of inhibitors of tumor cell growth, as it can either potentiate the effects of radiotherapy and conventional genotoxins or exploit synthetic lethal interactions
medicine
UBE2L3 might be a potential therapeutic target to treat SLE and B-cell lymphomas that are characterized by LUBAC hyperactivation and constitutive NF-kappaB signalling
REF.
AUTHORS
TITLE
JOURNAL
VOL.
PAGES
YEAR
ORGANISM (UNIPROT)
PUBMED ID
SOURCE
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 (P62837), 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
Manually annotated by BRENDA team
Plafker, K.S.; Nguyen, L.; Barneche, M.; Mirza, S.; Crawford, D.; Plafker, S.M.
The ubiquitin-conjugating enzyme UbcM2 can regulate the stability and activity of the antioxidant transcription factor Nrf2
J. Biol. Chem.
285
23064-23074
2010
Homo sapiens
Manually annotated by BRENDA team
van Wijk, S.J.; Timmers, H.T.
The family of ubiquitin-conjugating enzymes (E2s):deciding between life and death of proteins
FASEB J.
24
981-93
2010
Homo sapiens
Manually annotated by BRENDA team
David, Y.; Ziv, T.; Admon, A.; Navon, A.
The E2 ubiquitin-conjugating enzymes direct polyubiquitination to preferred lysines
J. Biol. Chem.
285
8595-8604
2010
Homo sapiens
Manually annotated by BRENDA team
Scaglione, K.M.; Basrur, V.; Ashraf, N.S.; Konen, J.R.; Elenitoba-Johnson, K.S.; Todi, S.V.; Paulson, H.L.
The ubiquitin-conjugating enzyme (E2) Ube2w ubiquitinates the N terminus of substrates
J. Biol. Chem.
288
18784-18788
2013
Homo sapiens
Manually annotated by BRENDA team
Tokgoez, Z.; Siepmann, T.J.; Streich, F.; Kumar, B.; Klein, J.M.; Haas, A.L.
E1-E2 interactions in ubiquitin and Nedd8 ligation pathways
J. Biol. Chem.
287
311-321
2012
Homo sapiens (P22314), Homo sapiens (Q8TBC4)
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 (P62837)
Manually annotated by BRENDA team
Tatham, M.; Kim, S.; Yu, B.; Jaffray, E.; Song, J.; Zheng, J.; Rodriguez, M.; Hay, R.; Chen, Y.
Role of an N-terminal site of Ubc9 in SUMO-1, -2, and -3 binding and conjugation
Biochemistry
42
9959-9969
2003
Homo sapiens (P63279)
Manually annotated by BRENDA team
Nguyen, L.; Plafker, K.S.; Starnes, A.; Cook, M.; Klevit, R.E.; Plafker, S.M.
The ubiquitin-conjugating enzyme, UbcM2, is restricted to monoubiquitylation by a two-fold mechanism that involves backside residues of E2 and Lys48 of ubiquitin
Biochemistry
53
4004-4014
2014
Homo sapiens (Q969T4)
Manually annotated by BRENDA team
Aichem, A.; Catone, N.; Groettrup, M.
Investigations into the auto-FAT10ylation of the bispecific E2 conjugating enzyme UBA6-specific E2 enzyme 1
FEBS J.
281
1848-1859
2014
Homo sapiens (Q9H832)
Manually annotated by BRENDA team
Zulkifle, N.
Systematic yeast two-hybrid analysis of human E2 ubiquitin-conjugating enzyme and deubiquitin (DUB) protein interactions
Int. J. Biol. Chem.
7
1-14
2013
Homo sapiens
-
Manually annotated by BRENDA team
Yokota, K.; Shibata, H.; Kurihara, I.; Kobayashi, S.; Suda, N.; Murai-Takeda, A.; Saito, I.; Kitagawa, H.; Kato, S.; Saruta, T.; Itoh, H.
Coactivation of the N-terminal transactivation of mineralocorticoid receptor by Ubc9
J. Biol. Chem.
282
1998-2010
2007
Homo sapiens
Manually annotated by BRENDA team
Park, Y.; Yoon, S.K.; Yoon, J.B.
The HECT domain of TRIP12 ubiquitinates substrates of the ubiquitin fusion degradation pathway
J. Biol. Chem.
284
1540-1549
2009
Homo sapiens (P51668)
Manually annotated by BRENDA team
Wang, Y.; Kim, S.M.; Trnka, M.J.; Liu, Y.; Burlingame, A.L.; Correia, M.A.
Human liver cytochrome P450 3A4 ubiquitination: molecular recognition by UBC7-gp78 autocrine motility factor receptor and UbcH5a-CHIP-Hsc70-Hsp40 E2-E3 ubiquitin ligase complexes
J. Biol. Chem.
290
3308-3332
2015
Homo sapiens (P62253)
Manually annotated by BRENDA team
Fiesel, F.; Moussaud-Lamodiere, E.; Ando, M.; Springer, W.
A specific subset of E2 ubiquitin-conjugating enzymes regulate Parkin activation and mitophagy differently
J. Cell Sci.
127
3488-3504
2014
Homo sapiens
Manually annotated by BRENDA team
Wang, D.; Tian, Y.; Wei, D.; Jing, Y.; Niu, H.; Xie, K.; Song, Y.
DNA Damage-induced foci of E2 ubiquitin-conjugating enzyme are detectable upon co-transfection with an interacting E3 ubiquitin ligase
Biochem. Genet.
54
147-157
2015
Homo sapiens
Manually annotated by BRENDA team
Goodman, S.; Petrofes Chapa, R.; Zimmer, W.
Spectrin's chimeric E2/E3 enzymatic activity
Exp. Biol. Med.
240
1039-1049
2015
Homo sapiens
Manually annotated by BRENDA team
Chakrabarti, K.S.; Li, J.; Das, R.; Byrd, R.A.
Conformational dynamics and allostery in E2 E3 interactions drive ubiquitination gp78 and Ube2g2
Structure
25
794-805
2017
Homo sapiens (P60604)
Manually annotated by BRENDA team
Hewitt, W.M.; Lountos, G.T.; Zlotkowski, K.; Dahlhauser, S.D.; Saunders, L.B.; Needle, D.; Tropea, J.E.; Zhan, C.; Wei, G.; Ma, B.; Nussinov, R.; Waugh, D.S.; Schneekloth, J.S.
Insights into the allosteric inhibition of the SUMO E2 enzyme Ubc9
Angew. Chem. Int. Ed. Engl.
55
5703-5707
2016
Homo sapiens (P63279)
Manually annotated by BRENDA team
Tan, J.M.E.; Cook, E.C.L.; van den Berg, M.; Scheij, S.; Zelcer, N.; Loregger, A.
Differential use of E2 ubiquitin conjugating enzymes for regulated degradation of the rate-limiting enzymes HMGCR and SQLE in cholesterol biosynthesis
Atherosclerosis
281
137-142
2019
Homo sapiens (P60604), Homo sapiens (Q8N2K1), Homo sapiens (Q9Y385), Homo sapiens
Manually annotated by BRENDA team
Wang, D.; Tian, Y.; Wei, D.; Jing, Y.; Niu, H.; Xie, K.; Song, Y.
DNA damage-induced foci of E2 ubiquitin-conjugating enzyme are detectable upon co-transfection with an interacting E3 ubiquitin ligase
Biochem. Genet.
54
147-157
2016
Homo sapiens (P49459), Homo sapiens (P63146)
Manually annotated by BRENDA team
Alpi, A.F.; Chaugule, V.; Walden, H.
Mechanism and disease association of E2-conjugating enzymes lessons from UBE2T and UBE2L3
Biochem. J.
473
3401-3419
2016
Homo sapiens (P68036), Homo sapiens (Q9NPD8)
Manually annotated by BRENDA team
Hsu, S.H.; Chen, S.H.; Kuo, C.C.; Chang, J.Y.
Ubiquitin-conjugating enzyme E2 B regulates the ubiquitination of O6-methylguanine-DNA methyltransferase and BCNU sensitivity in human nasopharyngeal carcinoma cells
Biochem. Pharmacol.
158
327-338
2018
Homo sapiens (P63146), Homo sapiens
Manually annotated by BRENDA team
Stewart, M.D.; Ritterhoff, T.; Klevit, R.E.; Brzovic, P.S.
E2 enzymes more than just middle men
Cell Res.
26
423-440
2016
Homo sapiens (A1L167), Homo sapiens (O00762), Homo sapiens (O14933), Homo sapiens (P49427), Homo sapiens (P49459), Homo sapiens (P51668), Homo sapiens (P51965), Homo sapiens (P60604), Homo sapiens (P61077), Homo sapiens (P61086), Homo sapiens (P61088), Homo sapiens (P62253), Homo sapiens (P62256), Homo sapiens (P62837), Homo sapiens (P63146), Homo sapiens (P68036), Homo sapiens (Q13404), Homo sapiens (Q15819), Homo sapiens (Q16763), Homo sapiens (Q5JXB2), Homo sapiens (Q5VVX9), Homo sapiens (Q712K3), Homo sapiens (Q7Z7E8), Homo sapiens (Q8N2K1), Homo sapiens (Q8WVN8), Homo sapiens (Q969T4), Homo sapiens (Q96LR5), Homo sapiens (Q9H832), Homo sapiens (Q9NPD8), Homo sapiens (Q9Y385)
Manually annotated by BRENDA team
Mizushima, N.
The ubiquitin E2 enzyme UBE2QL1 mediates lysophagy
EMBO Rep.
20
e49104
2019
Homo sapiens (A1L167)
Manually annotated by BRENDA team
Schelpe, J.; Monte, D.; Dewitte, F.; Sixma, T.; Rucktooa, P.
Structure of UBE2Z enzyme provides functional insight into specificity in the FAT10 protein conjugation machinery
J. Biol. Chem.
291
630-639
2016
Homo sapiens (Q9H832)
Manually annotated by BRENDA team
Lei, L.; Bandola-Simon, J.; Roche, P.A.
Ubiquitin-conjugating enzyme E2 D1 (Ube2D1) mediates lysine-independent ubiquitination of the E3 ubiquitin ligase March-I
J. Biol. Chem.
293
3904-3912
2018
Homo sapiens (P51668)
Manually annotated by BRENDA team
van de Weijer, M.L.; Schuren, A.B.C.; van den Boomen, D.J.H.; Mulder, A.; Claas, F.H.J.; Lehner, P.J.; Lebbink, R.J.; Wiertz, E.J.H.J.
Multiple E2 ubiquitin-conjugating enzymes regulate human cytomegalovirus US2-mediated immunoreceptor downregulation
J. Cell Sci.
130
2883-2892
2017
Homo sapiens (P60604), Homo sapiens (P61077), Homo sapiens (Q8N2K1), Homo sapiens
Manually annotated by BRENDA team
Morreale, F.E.; Bortoluzzi, A.; Chaugule, V.K.; Arkinson, C.; Walden, H.; Ciulli, A.
Allosteric targeting of the Fanconi anemia ubiquitin-conjugating enzyme Ube2T by fragment screening
J. Med. Chem.
60
4093-4098
2017
Homo sapiens (Q9NPD8)
Manually annotated by BRENDA team
Hill, S.; Harrison, J.S.; Lewis, S.M.; Kuhlman, B.; Kleiger, G.
Mechanism of lysine 48 selectivity during polyubiquitin chain formation by the Ube2R1/2 ubiquitin-conjugating enzyme
Mol. Cell. Biol.
36
1720-1732
2016
Homo sapiens (P49427), Homo sapiens (Q712K3)
Manually annotated by BRENDA team
Williams, K.M.; Qie, S.; Atkison, J.H.; Salazar-Arango, S.; Alan Diehl, J.; Olsen, S.K.
Structural insights into E1 recognition and the ubiquitin-conjugating activity of the E2 enzyme Cdc34
Nat. Commun.
10
3296
2019
Saccharomyces cerevisiae (P14682), Homo sapiens (P49427), Saccharomyces cerevisiae ATCC 204508 (P14682)
Manually annotated by BRENDA team
Rout, M.K.; Lee, B.L.; Lin, A.; Xiao, W.; Spyracopoulos, L.
Active site gate dynamics modulate the catalytic activity of the ubiquitination enzyme E2-25K
Sci. Rep.
8
7002
2018
Homo sapiens (P61086)
Manually annotated by BRENDA team
Yu, H.; Xiang, P.; Pan, Q.; Huang, Y.; Xie, N.; Zhu, W.
Ubiquitin-conjugating enzyme E2T is an independent prognostic factor and promotes gastric cancer progression
Tumour Biol.
37
11723-11732
2016
Homo sapiens (Q9NPD8)
Manually annotated by BRENDA team