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Information on EC 2.3.2.24 - (E3-independent) E2 ubiquitin-conjugating enzyme and Organism(s) Homo sapiens and UniProt Accession P49459

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EC Tree
     2 Transferases
         2.3 Acyltransferases
             2.3.2 Aminoacyltransferases
                2.3.2.24 (E3-independent) E2 ubiquitin-conjugating enzyme
IUBMB Comments
The enzyme transfers a single ubiquitin directly from an ubiquitinated E1 ubiquitin-activating enzyme to itself, and on to a lysine residue of the acceptor protein without involvement of E3 ubiquitin transferases (cf. EC 2.3.2.26, EC 2.3.2.27). It forms a labile ubiquitin adduct in the presence of E1, ubiquitin, and Mg2+-ATP and catalyses the conjugation of ubiquitin to protein substrates, independently of E3. This transfer has only been observed with small proteins. In vitro a transfer to small acceptors (e.g. L-lysine, N-acetyl-L-lysine methyl ester) has been observed .
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Homo sapiens
UNIPROT: P49459
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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
hide(Overall reactions are displayed. Show all >>)
[E1 ubiquitin-activating enzyme]-S-ubiquitinyl-L-cysteine
+
[acceptor protein]-L-lysine
=
[E1 ubiquitin-activating enzyme]-L-cysteine
+
[acceptor protein]-N6-monoubiquitinyl-L-lysine
Synonyms
ube2o, e2-230k, e2-epf ubiquitin carrier protein, ubiquitin carrier protein e2, ubiquitin-conjugating enzyme e2 variant 1, ubiquitin-conjugating enzyme e2 n, ubiquitin-conjugating enzyme e2 c, ubiquitin-conjugating enzyme e2 e1, ubiquitin-conjugating enzyme e2 l3, ubiquitin-conjugating enzyme e2 variant 2, more
SYNONYM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
ubiquitin carrier protein A
-
ubiquitin-conjugating enzyme E2 A
-
biquitin carrier protein D4
-
biquitin-conjugating enzyme E2 T
-
E2 ubiquitin-conjugating enzyme
-
-
E2-EPF ubiquitin carrier protein
-
E2-EPF UCP
-
E2/E3 hybrid enzyme
-
N-terminus-conjugating E2
-
ubiquitin carrier protein B
-
ubiquitin carrier protein C
-
ubiquitin carrier protein D1
-
ubiquitin carrier protein D2
-
ubiquitin carrier protein D3
-
Ubiquitin carrier protein E1
-
ubiquitin carrier protein E2
-
ubiquitin carrier protein E3
-
Ubiquitin carrier protein G1
-
Ubiquitin carrier protein G2
-
ubiquitin carrier protein H
-
Ubiquitin carrier protein L3
-
ubiquitin carrier protein N
-
Ubiquitin carrier protein Q2
-
ubiquitin carrier protein R2
-
ubiquitin carrier protein S
-
ubiquitin carrier protein T
-
ubiquitin carrier protein W
-
ubiquitin-conjugating enzyme E2
-
ubiquitin-conjugating enzyme E2 B
-
ubiquitin-conjugating enzyme E2 C
-
ubiquitin-conjugating enzyme E2 D1
-
ubiquitin-conjugating enzyme E2 D2
-
ubiquitin-conjugating enzyme E2 D3
-
ubiquitin-conjugating enzyme E2 D4
-
ubiquitin-conjugating enzyme E2 E1
-
ubiquitin-conjugating enzyme E2 E2
-
ubiquitin-conjugating enzyme E2 E3
-
ubiquitin-conjugating enzyme E2 G1
-
ubiquitin-conjugating enzyme E2 G2
-
ubiquitin-conjugating enzyme E2 H
-
ubiquitin-conjugating enzyme E2 K
-
ubiquitin-conjugating enzyme E2 L3
-
ubiquitin-conjugating enzyme E2 N
-
ubiquitin-conjugating enzyme E2 O
-
Ubiquitin-conjugating enzyme E2 Q2
-
ubiquitin-conjugating enzyme E2 R1
-
ubiquitin-conjugating enzyme E2 R2
-
ubiquitin-conjugating enzyme E2 S
-
ubiquitin-conjugating enzyme E2 variant 1
-
ubiquitin-conjugating enzyme E2 variant 2
-
ubiquitin-conjugating enzyme E2 W
-
ubiquitin-conjugating enzyme E2-25 kDa
-
ubiquitin-conjugating enzyme E2-CDC34
-
REACTION
REACTION DIAGRAM
COMMENTARY hide
ORGANISM
UNIPROT
LITERATURE
[E1 ubiquitin-activating enzyme]-S-ubiquitinyl-L-cysteine + [acceptor protein]-L-lysine = [E1 ubiquitin-activating enzyme]-L-cysteine + [acceptor protein]-N6-monoubiquitinyl-L-lysine
show the reaction diagram
E2 enzymes autoubiquitinate both their active sites cysteine and lysine residues, the latter described for this enzyme. E2 enzymes catalyze polyubiquitin formation with a specific lysine preference or a limited subset of lysine residues of ubiquitin. Accepts ubiquitin from the E1 complex and catalyzes its covalent attachment to other proteins. In vitro catalyzes Lys11, as well as Lys48-linked polyubiquitination
[E1 ubiquitin-activating enzyme]-S-ubiquitinyl-L-cysteine + [acceptor protein]-L-lysine = [E1 ubiquitin-activating enzyme]-L-cysteine + [acceptor protein]-N6-monoubiquitinyl-L-lysine
show the reaction diagram
PATHWAY SOURCE
PATHWAYS
-
-
SYSTEMATIC NAME
IUBMB Comments
S-ubiquitinyl-[E1 ubiquitin-activating enzyme]-L-cysteine:L-lysine ubiquitinyl transferase ([E3 ubiquitin transferase]-independent)
The enzyme transfers a single ubiquitin directly from an ubiquitinated E1 ubiquitin-activating enzyme to itself, and on to a lysine residue of the acceptor protein without involvement of E3 ubiquitin transferases (cf. EC 2.3.2.26, EC 2.3.2.27). It forms a labile ubiquitin adduct in the presence of E1, ubiquitin, and Mg2+-ATP and catalyses the conjugation of ubiquitin to protein substrates, independently of E3. This transfer has only been observed with small proteins. In vitro a transfer to small acceptors (e.g. L-lysine, N-acetyl-L-lysine methyl ester) has been observed [1].
SUBSTRATE
PRODUCT                       
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate) hide
LITERATURE
(Substrate)
COMMENTARY
(Product) hide
LITERATURE
(Product)
Reversibility
r=reversible
ir=irreversible
?=not specified
2 N6-monoubiquitinyl-[Ube2K]-L-lysine
N6-diubiquitinyl-[Ube2K]-L-lysine + [Ube2K]-L-lysine
show the reaction diagram
-
-
-
?
S-ubiquitinyl-[E1 ubiquitin-activating enzyme]-L-cysteine + L-lysine
[E1 ubiquitin-activating enzyme]-L-cysteine + N6-monoubiquitinyl-L-lysine
show the reaction diagram
-
-
-
-
?
S-ubiquitinyl-[E1 ubiquitin-activating enzyme]-L-cysteine + S-(ubiquitin)n-Ube2g2-L-cysteine
[E1 ubiquitin-activating enzyme]-L-cysteine + S-(ubiquitin)(n+1)-Ube2g2-L-cysteine
show the reaction diagram
-
short chains of polyubiquitins can be linked bonds to E2 enzyme Ube2g2
-
?
S-ubiquitinyl-[E1 ubiquitin-activating enzyme]-L-cysteine + S-(ubiquitin)n-Ube2K-L-cysteine
[E1 ubiquitin-activating enzyme]-L-cysteine + S-(ubiquitin)(n+1)-Ube2K-L-cysteine
show the reaction diagram
-
longer chains of polyubiquitins can be linked bonds to E2 enzyme Ube2K. Ubiquitin chains are assembled on the active site cysteine of Ube2K through thioester bond
-
?
S-ubiquitinyl-[E1 ubiquitin-activating enzyme]-L-cysteine + UbcH10-L-cysteine
[E1 ubiquitin-activating enzyme]-L-cysteine + S-monoubiquitinyl-UbcH10-L-cysteine
show the reaction diagram
-
-
-
?
S-ubiquitinyl-[E1 ubiquitin-activating enzyme]-L-cysteine + Ube2g2-L-cysteine
[E1 ubiquitin-activating enzyme]-L-cysteine + S-monoubiquitinyl-Ube2g2-L-cysteine
show the reaction diagram
-
-
-
?
S-ubiquitinyl-[E1 ubiquitin-activating enzyme]-L-cysteine + Ube2K-L-cysteine
[E1 ubiquitin-activating enzyme]-L-cysteine + S-monoubiquitinyl-Ube2K-L-cysteine
show the reaction diagram
-
-
-
?
S-ubiquitinyl-[E1 ubiquitin-activating enzyme]-L-cysteine + [cytochrome c]-L-lysine
[E1 ubiquitin-activating enzyme]-L-cysteine + N6-monoubiquitinyl-[cytochrome c]-L-lysine lysine
show the reaction diagram
-
-
approximate relative activities as ubiquitin acceptors are: histones H2A:H2B:cytochrome c 1:0.5:0.2
-
?
S-ubiquitinyl-[E1 ubiquitin-activating enzyme]-L-cysteine + [histone H2A]-L-lysine
[E1 ubiquitin-activating enzyme]-L-cysteine + N6-monoubiquitinyl-[histone H2A]-L-lysine
show the reaction diagram
-
-
approximate relative activities as ubiquitin acceptors are: histones H2A:H2B:cytochrome c 1:0.5:0.2
-
?
S-ubiquitinyl-[E1 ubiquitin-activating enzyme]-L-cysteine + [histone H2B]-L-lysine
[E1 ubiquitin-activating enzyme]-L-cysteine + N6-monoubiquitinyl-[histone H2B]-L-lysine lysine
show the reaction diagram
-
-
approximate relative activities as ubiquitin acceptors are: histones H2A:H2B:cytochrome c 1:0.5:0.2
-
?
[E1 ubiquitin-activating enzyme]-S-ubiquitinyl-L-cysteine + [acceptor protein]-L-lysine
[E1 ubiquitin-activating enzyme]-L-cysteine + [acceptor protein]-N6-monoubiquitinyl-L-lysine
show the reaction diagram
[E1 ubiquitin-activating enzyme]-S-ubiquitinyl-L-cysteine + [AMPKalpha2]-L-lysine48
[E1 ubiquitin-activating enzyme]-L-cysteine + [AMPKalpha2 ]-N6-monoubiquitinyl-L-lysine48
show the reaction diagram
polyubiquitination of AMPKalpha2
-
-
?
[E1 ubiquitin-activating enzyme]-S-ubiquitinyl-L-cysteine + [AMPKalpha2]-L-lysine48
[E1 ubiquitin-activating enzyme]-L-cysteine + [AMPKalpha2]-N6-monoubiquitinyl-L-lysine48
show the reaction diagram
-
-
-
?
[E1 ubiquitin-activating enzyme]-S-ubiquitinyl-L-cysteine + [BAP1]-L-lysine
[E1 ubiquitin-activating enzyme]-L-cysteine + [BAP1]-N6-monoubiquitinyl-L-lysine
show the reaction diagram
UBE2O promotes multi-monoubiquitination on BAP1. The ubiquitination of BAP1 requires both the N-terminal CR1-CR2 domain and the C-terminal UBC domain of UBE2O. The absence of either domain completely abolishes BAP1 ubiquitination
-
-
?
[E1 ubiquitin-activating enzyme]-S-ubiquitinyl-L-cysteine + [BMAL1]-L-lysine
[E1 ubiquitin-activating enzyme]-L-cysteine + [BMAL1]-N6-monoubiquitinyl-L-lysine
show the reaction diagram
[E1 ubiquitin-activating enzyme]-S-ubiquitinyl-L-cysteine + [c-Maf]-L-lysine
[E1 ubiquitin-activating enzyme]-L-cysteine + [acceptor c-Maf]-N6-monoubiquitinyl-L-lysine
show the reaction diagram
polyubiquitination of o-Maf
-
-
?
[E1 ubiquitin-activating enzyme]-S-ubiquitinyl-L-cysteine + [Hippel-Lindau protein]-L-lysine
[E1 ubiquitin-activating enzyme]-L-cysteine + [Hippel-Lindau protein]-N6-monoubiquitinyl-L-lysine
show the reaction diagram
[E1 ubiquitin-activating enzyme]-S-ubiquitinyl-L-cysteine + [MLL protein]-L-lysine
[E1 ubiquitin-activating enzyme]-L-cysteine + [MLL protein]-N6-monoubiquitinyl-L-lysine
show the reaction diagram
polyubiquitination of protein MLL
-
-
?
[E1 ubiquitin-activating enzyme]-S-ubiquitinyl-L-cysteine + [SMAD6]-L-lysine
[E1 ubiquitin-activating enzyme]-L-cysteine + [SMAD6]-N6-monoubiquitinyl-L-lysine
show the reaction diagram
monoubiquitination of SMAD6
-
-
?
[E1 ubiquitin-activating enzyme]-S-ubiquitinyl-L-cysteine + [TRAF6]-L-lysine63
[E1 ubiquitin-activating enzyme]-L-cysteine + [TRAF6]-N6-monoubiquitinyl-L-lysine63
show the reaction diagram
polyubiquitination of TRAF6 K63
-
-
?
[ubiquitin-carrier protein UbcH2]-S-ubiquitinyl-L-cysteine + [Eps15]-L-lysine
[ubiquitin-carrier protein UbcH2]-L-cysteine + [Eps15]-N6-ubiquitinyl-L-lysine
show the reaction diagram
-
substrate protein Eps15 contains two C-terminal ubiquitin-interacting motifs. It is potently ubiquitinated by UbcH5 isoforms and less well by UbcH2 and UbcH6
-
-
?
[ubiquitin-carrier protein UbcH2]-S-ubiquitinyl-L-cysteine + [Pol k]-L-lysine
[ubiquitin-carrier protein UbcH2]-L-cysteine + [Pol k]-N6-ubiquitinyl-L-lysine
show the reaction diagram
-
substrate protein Pol k contains two C-terminal ubiquitin-binding zinc finger domains. It is ubiquitinated by UbcH2, UbcH5 isoforms and UbcH6
-
-
?
[ubiquitin-carrier protein UbcH5A]-S-ubiquitinyl-L-cysteine + [Stam2]-L-lysine
[ubiquitin-carrier protein UbcH5A]-L-cysteine + [Stam6]-N6-ubiquitinyl-L-lysine
show the reaction diagram
-
substrate protein Stam2 contains a N-terminal ubiquitin-interacting motif and VHS domain, it is most strongly ubiquitinated by E2 isoform UbcH5A
-
-
?
[ubiquitin-carrier protein UbcH5]-S-ubiquitinyl-L-cysteine + [Eps15]-L-lysine
[ubiquitin-carrier protein UbcH5]-L-cysteine + [Eps15]-N6-ubiquitinyl-L-lysine
show the reaction diagram
-
substrate protein Eps15 contains two C-terminal ubiquitin-interacting motifs. It is potently ubiquitinated by UbcH5 isoforms and less well by UbcH2 and UbcH6
-
-
?
[ubiquitin-carrier protein UbcH5]-S-ubiquitinyl-L-cysteine + [Pol k]-L-lysine
[ubiquitin-carrier protein UbcH5]-L-cysteine + [Pol k]-N6-ubiquitinyl-L-lysine
show the reaction diagram
-
substrate protein Pol k contains two C-terminal ubiquitin-binding zinc finger domains. It is ubiquitinated by UbcH2, UbcH5 isoforms and UbcH6
-
-
?
[ubiquitin-carrier protein UbcH5]-S-ubiquitinyl-L-cysteine + [Pol tau]-L-lysine
[ubiquitin-carrier protein UbcH5]-L-cysteine + [Pol tau]-N6-ubiquitinyl-L-lysine
show the reaction diagram
-
substrate protein Pol tau contains two C-terminal ubiquitin-associated domains. It is ubiquitinated by all E2 isoforms tested
-
-
?
[ubiquitin-carrier protein UbcH6]-S-ubiquitinyl-L-cysteine + [Eps15]-L-lysine
[ubiquitin-carrier protein UbcH6]-L-cysteine + [Eps15]-N6-ubiquitinyl-L-lysine
show the reaction diagram
-
substrate protein Eps15 contains two C-terminal ubiquitin-interacting motifs. It is potently ubiquitinated by UbcH5 isoforms and less well by UbcH2 and UbcH6
-
-
?
[ubiquitin-carrier protein UbcH6]-S-ubiquitinyl-L-cysteine + [Pol k]-L-lysine
[ubiquitin-carrier protein UbcH6]-L-cysteine + [Pol k]-N6-ubiquitinyl-L-lysine
show the reaction diagram
-
substrate protein Pol k contains two C-terminal ubiquitin-binding zinc finger domains. It is ubiquitinated by UbcH2, UbcH5 isoforms and UbcH6
-
-
?
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
[E1 ubiquitin-activating enzyme]-S-ubiquitinyl-L-cysteine + [acceptor protein]-L-lysine
[E1 ubiquitin-activating enzyme]-L-cysteine + [acceptor protein]-N6-monoubiquitinyl-L-lysine
show the reaction diagram
[E1 ubiquitin-activating enzyme]-S-ubiquitinyl-L-cysteine + [AMPKalpha2]-L-lysine48
[E1 ubiquitin-activating enzyme]-L-cysteine + [AMPKalpha2]-N6-monoubiquitinyl-L-lysine48
show the reaction diagram
-
-
-
?
[E1 ubiquitin-activating enzyme]-S-ubiquitinyl-L-cysteine + [BAP1]-L-lysine
[E1 ubiquitin-activating enzyme]-L-cysteine + [BAP1]-N6-monoubiquitinyl-L-lysine
show the reaction diagram
UBE2O promotes multi-monoubiquitination on BAP1. The ubiquitination of BAP1 requires both the N-terminal CR1-CR2 domain and the C-terminal UBC domain of UBE2O. The absence of either domain completely abolishes BAP1 ubiquitination
-
-
?
[E1 ubiquitin-activating enzyme]-S-ubiquitinyl-L-cysteine + [BMAL1]-L-lysine
[E1 ubiquitin-activating enzyme]-L-cysteine + [BMAL1]-N6-monoubiquitinyl-L-lysine
show the reaction diagram
mapping of the BMAL1-interacting domain in UBE2O
-
-
?
[E1 ubiquitin-activating enzyme]-S-ubiquitinyl-L-cysteine + [Hippel-Lindau protein]-L-lysine
[E1 ubiquitin-activating enzyme]-L-cysteine + [Hippel-Lindau protein]-N6-monoubiquitinyl-L-lysine
show the reaction diagram
-
-
-
?
ORGANISM
COMMENTARY hide
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
-
UniProt
Manually annotated by BRENDA team
SOURCE TISSUE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
SOURCE
UBE2O expression in cell lines and cancers, and UBE2O expression and mutation in cancers, detailed overview
Manually annotated by BRENDA team
additional information
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?
UBE2A_HUMAN
152
0
17315
Swiss-Prot
-
MOLECULAR WEIGHT
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
SUBUNIT
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
dimer
E2 enzymes spontaneously dimerize in solution, in vitro, in absence of charged ubiquitin
dimer
additional information
POSTTRANSLATIONAL MODIFICATION
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
phosphoprotein
UBE2O contains several potential phosphorylation sites and their phosphorylation may regulate UBE2O localization and its physiological roles
PROTEIN VARIANTS
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
C118A
site-directed mutagenesis, inactive mutant
C95A
site-directed mutagenesis, the mutant shows impaired ubiquination activity
K76R/K100R
site-directed mutagenesis, the mutant shows reduced autoubiquitination activity compared to wild-type
additional information
PURIFICATION (Commentary)
ORGANISM
UNIPROT
LITERATURE
recombinant tagged wild-type and mutant UCP enzymes by affinity chromatography from HEK-293T cells
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 and transformed into Escherichia coli (BL-21 DE3) using pET22 vector in frame to a C-terminal His6 tag
gene UBE2O, cloned from liver, DNA and amino acid sequence determination and comparisons
gene UBE2O, recombinant expression of Strep-tagged UBE2O in HEK-293 cells, coexpression with FLAG-tagged BMAL1 transcription factor
recombinant expression of diversely tagged wild-type and mutant UCP enzymes in HEK-293T cells, the activity of the recombinant mutant enzymes varies dependent on the fusion tag, overview
APPLICATION
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
diagnostics
high expression of UBE2O is associated with low survival rate of gastric, lung, breast, and prostate cancer patients
drug development
E2 ubiquitin-conjugating enzymes might be potential drug targets, potential strategies for drug discovery targeting UBE2O, overview
REF.
AUTHORS
TITLE
JOURNAL
VOL.
PAGES
YEAR
ORGANISM (UNIPROT)
PUBMED ID
SOURCE
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, Homo sapiens (O00762), 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 (Q712K3), Homo sapiens (Q8WVN8), Homo sapiens (Q969T4), Homo sapiens (Q96B02), Homo sapiens (Q96LR5), Homo sapiens (Q9NPD8), Homo sapiens (Q9Y2X8)
Manually annotated by BRENDA team
Hoeller, D.; Hecker, C.M.; Wagner, S.; Rogov, V.; Doetsch, V.; Dikic, I.
E3-independent monoubiquitination of ubiquitin-binding proteins
Mol. Cell
26
891-898
2007
Homo sapiens
Manually annotated by BRENDA team
Shin, D.Y.; Lee, H.; Park, E.S.; Yoo, Y.J.
Assembly of different length of polyubiquitins on the catalytic cysteine of E2 enzymes without E3 ligase; a novel application of non-reduced/reduced 2-dimensional electrophoresis
FEBS Lett.
585
3959-3963
2011
Homo sapiens (O00762), Homo sapiens (P60604), Homo sapiens (P61086)
Manually annotated by BRENDA team
Pickart, C.M.; Rose, I.A.
Functional heterogeneity of ubiquitin carrier proteins
J. Biol. Chem.
260
1573-1581
1985
Homo sapiens
Manually annotated by BRENDA team
Cook, B.W.; Barber, K.R.; Shilton, B.H.; Shaw, G.S.
The HIP2-ubiquitin conjugate forms a non-compact monomeric thioester during di-ubiquitin synthesis
PLoS ONE
10
e0120318
2015
Saccharomyces cerevisiae (P21734), Homo sapiens (P61086)
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 (Q9C0C9)
Manually annotated by BRENDA team
Ullah, K.; Zubia, E.; Narayan, M.; Yang, J.; Xu, G.
Diverse roles of the E2/E3 hybrid enzyme UBE2O in the regulation of protein ubiquitination, cellular functions, and disease onset
FEBS J.
286
2018-2034
2019
Homo sapiens (Q9C0C9), Homo sapiens
Manually annotated by BRENDA team
Chen, S.; Yang, J.; Zhang, Y.; Duan, C.; Liu, Q.; Huang, Z.; Xu, Y.; Zhou, L.; Xu, G.
Ubiquitin-conjugating enzyme UBE2O regulates cellular clock function by promoting the degradation of the transcription factor BMAL1
J. Biol. Chem.
293
11296-11309
2018
Homo sapiens (Q9C0C9), Homo sapiens
Manually annotated by BRENDA team
Lim, J.; Shin, H.; Chung, K.; Kim, N.; Kim, J.; Jung, H.; Im, D.; Jung, C.
E2-EPF UCP possesses E3 ubiquitin ligase activity via its cysteine 118 residue
PLoS ONE
11
e0163710
2016
Homo sapiens (Q9C0C9)
Manually annotated by BRENDA team