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Information on EC 2.3.2.23 - E2 ubiquitin-conjugating enzyme
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2.3.2.23 E2 ubiquitin-conjugating enzymeIUBMB 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.
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Word Map
- 2.3.2.23
- proteasome
- ligases
-
polyubiquitination
-
sumoylation
-
ubiquitin-like
- finger
-
ubiquitin-proteasome
-
ubiquitylation
-
monoubiquitination
- ubiquitin-protein
-
ubiquitin-activating
-
k63-linked
-
ubiquitin-dependent
-
cullins
- parkin
-
ubiquitin-mediated
-
ubiquitin-related
-
fanconi
-
anaphase-promoting
-
deubiquitinating
-
cullin-ring
-
isopeptide
-
error-free
- isg15
-
lys63-linked
-
neddylation
- cdc20
- sumo1
-
autoubiquitination
- traf6
-
er-associated
-
ring-h2
- ranbp2
- tak1
- thiolester
-
ring-finger
- sic1
-
e3-ligase
-
multiubiquitination
- tpx2
- rbx1
-
translesion
-
fancd2
-
aurka
-
postreplication
-
conjugase
-
ubiquitin-binding
-
ubiquitin-ligase
-
ring-type
- medicine
-
nonerythroid
- diagnostics
- drug development
The enzyme appears in 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, 
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SYNONYM 
ORGANISM
UNIPROT
COMMENTARY 
LITERATURE
CDC34
E2 enzyme
E2 ubiquitin-conjugating enzyme
E2-ubiquitin conjugating enzyme
Rad6p
SUMO-conjugating enzyme UBC9
Ubc1
Ubc11
Ubc13
Ubc2
UBC7
Ubc9
UbcH5A
UbcH7
UbcH8
UbcM2
Ube2
Ube2J1
UBE2L3
UBE2N
UBE2R1
UBE2T
ubiquitin-conjugating enzyme
ubiquitin-conjugating enzyme E2
ubiquitin-conjugating enzyme E2-20 kDa
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REACTION
REACTION DIAGRAM
COMMENTARY
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
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
E2 enzymes autoubiquitinate both their active sites cysteine, described for this enzyme and lysine residues
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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
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REACTION TYPE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
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PATHWAY SOURCE
PATHWAYS
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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.
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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-SUMOyl-[E1 SUMO-activating enzyme]-L-cysteine + [Ubc9]-L-cysteine
[E1 SUMO-activating enzyme]-L-cysteine + S-SUMOyl-[Ubc9]-L-cysteine
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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
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?
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
S-ubiquitinyl-[Uba1]-L-cysteine + [Ubc5a]-L-cysteine
[Uba1]-L-cysteine + S-ubiquitinyl-[Ubc5a]-L-cysteine
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the E1 enzyme Uba1, the E2 enzyme UbcH5a, and the E3 enzyme TRIP12 are responsible for ubiquitylation of ubiquitin mutant G76V
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?
[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
binding of Ubc4 to the E1ubiquitin 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
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?
[ubiquitin-activating protein E1]-S-ubiquitinyl-L-cysteine + [ubiquitin carrier protein UbcH7]-L-cysteine
[ubiquitin-activating protein E1]-L-cysteine + [ubiquitin carrier protein UbcH7]-S-ubiquitinyl-L-cysteine
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-
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?
[ubiquitin-activating protein E1]-S-ubiquitinyl-L-cysteine + [ubiquitin-carrier-protein Ube2r]-L-cysteine
[ubiquitin-activating protein E1]-L-cysteine + [ubiquitin-carrier-protein Ube2r]-S-ubiquitinyl-L-cysteine
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enzyme is capable of forming a thiolester bond with ubiquitin
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?
[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
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?
[ubiquitin-activating protein UBA1]-S-ubiquitinyl-L-cysteine + [ubiquitin carrier protein E2]-L-cysteine
[ubiquitin-activating protein BA1]-L-cysteine + [ubiquitin carrier protein E2]-S-ubiquitinyl-L-cysteine
transfer of ubiquitin from activating protein UBA1 can take place to different ubiquitin-carrier enzymes E2, with little discrimination for the type of E2 protein
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?
[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
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?
[ubiquitin-activating protein UBA2]-S-ubiquitinyl-L-cysteine + [ubiquitin carrier protein E2]-L-cysteine
[ubiquitin-activating protein UBA2]-L-cysteine + [ubiquitin carrier protein E2]-S-ubiquitinyl-L-cysteine
transfer of activated ubiquitin from E1 enzyme UBA2 is carried out to different ubiquitin-carrier enzymes E2, with little discrimination for the type of E2 protein
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?
[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
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?
[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
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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
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?
[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
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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
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?
[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
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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
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?
[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
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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
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?
[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
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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
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?
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
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-
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?
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
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?
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
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?
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
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?
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
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-
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?
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
A1L167, O00762, O14933, P49427, P49459, P51668, P51965, P60604, P61077, P61086, P61088, P62253, P62256, P62837, P63146, P68036, Q13404, Q15819, Q16763, Q5JXB2, Q5VVX9, Q712K3, Q7Z7E8, Q8N2K1, Q8WVN8, Q969T4, Q96LR5, Q9H832, Q9NPD8, Q9Y385
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?
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
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-
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?
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
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?
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
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?
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
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?
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
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?
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
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?
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
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-
-
?
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
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-
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?
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
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?
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
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?
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
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?
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
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erythrocyte spectrin has a chimeric E2/E3 ubiquitin-conjugating/ligating activity, which is capable of ubiquitinating itself
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?
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
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the enzyme ubiquitinates the N terminus of substrates
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?
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
K48- and K63-linked ubiquitination
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?
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
acceptor ubiquitin residue Arg54 participated in Ube2R1-catalyzed Lys 48 polyubiquitin chain formation. Significance of the Asp143 Ube2R1/2-Arg54 acceptor ubiquitin ion pair
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?
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
acceptor ubiquitin residue Arg54 participates in Ube2R1-catalyzed Lys48 polyubiquitin chain formation. Significance of the Asp143 Ube2R1/2-Arg54 acceptor ubiquitin ion pair
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?
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
A1L167, O00762, O14933, P49427, P49459, P51668, P51965, P60604, P61077, P61086, P61088, P62253, P62256, P62837, P63146, P68036, Q13404, Q15819, Q16763, Q5JXB2, Q5VVX9, Q712K3, Q7Z7E8, Q8N2K1, Q8WVN8, Q969T4, Q96LR5, Q9H832, Q9NPD8, Q9Y385
backside interaction was of Ub non-covalently bound to Ube2D3 via the hydrophobic patch centered on I44, a Ub surface used in many different protein-protein interactions. Although weak in affinity, the interaction promotes an increase in processivity of polyUb chain building by Ube2D3
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?
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
E2 loading reaction assay using ubiquitin D, i.e. FAT10, UniProt ID O15205. UBE2Z is specific for E1-like ubiquitin-activating enzyme UBA6. UBE2Z N-terminal extension and loop LB are essential for selectivity toward UBA6. UBA6 charges UBE2Z with FAT10 less efficiently than with ubiquitin. The C-terminal CYCI peptide in rFAT10 limits transfer Rates onto UBE2Z
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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
the E2 ubiquitin-conjugating enzyme acquires the activated ubquitin from the E1 ubiquitin-activating enzyme
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?
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
ubiquitin K48- and K63-linked ubiquitination
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?
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
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?
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
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?
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
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?
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
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?
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
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?
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
the E2 ubiquitin-conjugating enzyme acquires the activated ubquitin from the E1 ubiquitin-activating enzyme
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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
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?
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
the E2 ubiquitin-conjugating enzyme acquires the activated ubquitin from the E1 ubiquitin-activating enzyme
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?
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
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?
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
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?
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
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additional information
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HECT-E3 ligase ETC-1 ubiquitylates securin IFY-1 and cyclin B1 in the presence of the E2 enzyme UBC-18
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additional information
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HECT-E3 ligase ETC-1 ubiquitylates securin IFY-1 and cyclin B1 in the presence of the E2 enzyme UBC-18
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additional information
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polyubiquitin chain formation catalyzed by E2 enzymes, in the absence of an E3 protein and a target protein substrate
a thiol ester-linked ubiquitin to the E2 active site is an intermediate in any polyubiquination reactions
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additional information
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functional survey of 11 representative human E2 paralogs reveals similar Km values for binding to human Uba1 ternary complex with an average Km of 121 nM and kcat for ubiquitin transfer of 4.0 per s, suggesting that they possess a conserved binding site and transition state geometry and that they compete for charging through differences in intracellular concentration. This binding motif is localized to three basic residues within Helix 1 of the E2 core domain
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additional information
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functional survey of 11 representative human E2 paralogs reveals similar Km values for binding to human Uba1 ternary complex with an average Km of 121 nM and kcat for ubiquitin transfer of 4.0 per s, suggesting that they possess a conserved binding site and transition state geometry and that they compete for charging through differences in intracellular concentration. This binding motif is localized to three basic residues within Helix 1 of the E2 core domain
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additional information
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kinetics for Uba1a-catalyzed transthiolation of Ubc2b are used as a reporter assay for determining the Km and kcat values for the three cosubstrates of the ubiquitin-activating enzyme. The E2 transthiolation assays are more sensitive to the potential presence of trace catalytically active fragments than the single turnover end point assays used for quantitating ternary complex stoichiometry
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additional information
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during transfer of ubiquitin to the final substrate or E3 ligase, reaction of EC 2.3.2.27, enzyme is restricted to monoubiquitinylation. UbcM2 shows enhanced polyubiquitin synthesizing activity in reaction mixtures containing ubiquitin mutant K48R. In contrast, reaction mixtures containing ubiquitin mutant K6R show a mild suppression of UbcM2 activity
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additional information
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human liver endoplasmic reticulum-anchored cytochrome P450 enzyme CYP3A4 is degraded via ubiquitylation by E2 ubiquitin-conjugating enzyme UBC7/E3 ubiquitin-ligase gp78, reaction of EC 2.3.2.27. CYP3A4 Asp/Glu/Ser(P)/Thr(P) surface clusters are important for its intermolecular electrostatic interactions with each of these E2-E3 subcomponents. By imparting additional negative charge to these Asp/Glu clusters, such Ser/Thr phosphorylation would generate P450 phosphodegrons for molecular recognition by the E2-E3 complexes, thereby controlling the timing of CYP3A4 ubiquitination and endoplasmic reticulum-associated degradation
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additional information
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determination of the E1 catalyzed E2-25K-Ub thioester conjugation reaction
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additional information
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diubiquitin synthesis by enzyme UBE2R2 with 32P-labeled K48R donor ubiquitin and acceptor ubiquitin, which contains an additional Asp residue at its C-terminus (referred to as D77 ubiquitin, which cannot be thioesterified to Ube2R2), analysis of activities of wild-type Ube2R2 and mutants, D143K, D143R, D143A, and D91K, with wild-type ubiquitin and mutant ubiquitins, R54D, R54A, I44A, I44D, and D58R. The mutations reduce the activity, the combination of D143K enzyme with D58R ubiquitin is inactive, the mutation of Arg54 to an Asp residue in acceptor ubiquitin leads to a 52fold reduction in Ube2R2 activity compared with wild-type ubiquitin results. The Ube2R1/2 acidic loop participates in Lys48-specific polyubiquitin chain formation by binding to Skp1-cullin-Fbox (SCF), kinetics
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additional information
?
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diubiquitin synthesis by enzyme UBE2R2 with 32P-labeled K48R donor ubiquitin and acceptor ubiquitin, which contains an additional Asp residue at its C-terminus (referred to as D77 ubiquitin, which cannot be thioesterified to Ube2R2), analysis of activities of wild-type Ube2R2 and mutants, D143K, D143R, D143A, and D91K, with wild-type ubiquitin and mutant ubiquitins, R54D, R54A, I44A, I44D, and D58R. The mutations reduce the activity, the combination of D143K enzyme with D58R ubiquitin is inactive, the mutation of Arg54 to an Asp residue in acceptor ubiquitin leads to a 52fold reduction in Ube2R2 activity compared with wild-type ubiquitin results. The Ube2R1/2 acidic loop participates in Lys48-specific polyubiquitin chain formation by binding to Skp1-cullin-Fbox (SCF), kinetics
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additional information
?
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enzyme UBE2V1 and homologues are catalytically inactive E2-like proteins interacting with Ube2N for K63 chain formation. The enzyme interacts with ubiquitin, and with E3 ligases of types RING, and HECT (in combination with Ube2N). Whereas K63-specific Ube2N uses a tightly bound E2-like subunit (either Ube2V1 or Ube2V2) to position the K63 side chain of the incoming (acceptor) Ub
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-
-
additional information
?
-
enzyme UBE2V1 and homologues are catalytically inactive E2-like proteins interacting with Ube2N for K63 chain formation. The enzyme interacts with ubiquitin, and with E3 ligases of types RING, and HECT (in combination with Ube2N). Whereas K63-specific Ube2N uses a tightly bound E2-like subunit (either Ube2V1 or Ube2V2) to position the K63 side chain of the incoming (acceptor) Ub
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-
additional information
?
-
enzyme UBE2V1 and homologues are catalytically inactive E2-like proteins interacting with Ube2N for K63 chain formation. The enzyme interacts with ubiquitin, and with E3 ligases of types RING, and HECT (in combination with Ube2N). Whereas K63-specific Ube2N uses a tightly bound E2-like subunit (either Ube2V1 or Ube2V2) to position the K63 side chain of the incoming (acceptor) Ub
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additional information
?
-
enzyme UBE2V1 and homologues are catalytically inactive E2-like proteins interacting with Ube2N for K63 chain formation. The enzyme interacts with ubiquitin, and with E3 ligases of types RING, and HECT (in combination with Ube2N). Whereas K63-specific Ube2N uses a tightly bound E2-like subunit (either Ube2V1 or Ube2V2) to position the K63 side chain of the incoming (acceptor) Ub
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-
-
additional information
?
-
enzyme UBE2V1 and homologues are catalytically inactive E2-like proteins interacting with Ube2N for K63 chain formation. The enzyme interacts with ubiquitin, and with E3 ligases of types RING, and HECT (in combination with Ube2N). Whereas K63-specific Ube2N uses a tightly bound E2-like subunit (either Ube2V1 or Ube2V2) to position the K63 side chain of the incoming (acceptor) Ub
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-
-
additional information
?
-
enzyme UBE2V1 and homologues are catalytically inactive E2-like proteins interacting with Ube2N for K63 chain formation. The enzyme interacts with ubiquitin, and with E3 ligases of types RING, and HECT (in combination with Ube2N). Whereas K63-specific Ube2N uses a tightly bound E2-like subunit (either Ube2V1 or Ube2V2) to position the K63 side chain of the incoming (acceptor) Ub
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-
-
additional information
?
-
enzyme UBE2V1 and homologues are catalytically inactive E2-like proteins interacting with Ube2N for K63 chain formation. The enzyme interacts with ubiquitin, and with E3 ligases of types RING, and HECT (in combination with Ube2N). Whereas K63-specific Ube2N uses a tightly bound E2-like subunit (either Ube2V1 or Ube2V2) to position the K63 side chain of the incoming (acceptor) Ub
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-
-
additional information
?
-
enzyme UBE2V1 and homologues are catalytically inactive E2-like proteins interacting with Ube2N for K63 chain formation. The enzyme interacts with ubiquitin, and with E3 ligases of types RING, and HECT (in combination with Ube2N). Whereas K63-specific Ube2N uses a tightly bound E2-like subunit (either Ube2V1 or Ube2V2) to position the K63 side chain of the incoming (acceptor) Ub
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-
-
additional information
?
-
enzyme UBE2V1 and homologues are catalytically inactive E2-like proteins interacting with Ube2N for K63 chain formation. The enzyme interacts with ubiquitin, and with E3 ligases of types RING, and HECT (in combination with Ube2N). Whereas K63-specific Ube2N uses a tightly bound E2-like subunit (either Ube2V1 or Ube2V2) to position the K63 side chain of the incoming (acceptor) Ub
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-
-
additional information
?
-
enzyme UBE2V1 and homologues are catalytically inactive E2-like proteins interacting with Ube2N for K63 chain formation. The enzyme interacts with ubiquitin, and with E3 ligases of types RING, and HECT (in combination with Ube2N). Whereas K63-specific Ube2N uses a tightly bound E2-like subunit (either Ube2V1 or Ube2V2) to position the K63 side chain of the incoming (acceptor) Ub
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-
-
additional information
?
-
enzyme UBE2V1 and homologues are catalytically inactive E2-like proteins interacting with Ube2N for K63 chain formation. The enzyme interacts with ubiquitin, and with E3 ligases of types RING, and HECT (in combination with Ube2N). Whereas K63-specific Ube2N uses a tightly bound E2-like subunit (either Ube2V1 or Ube2V2) to position the K63 side chain of the incoming (acceptor) Ub
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-
-
additional information
?
-
enzyme UBE2V1 and homologues are catalytically inactive E2-like proteins interacting with Ube2N for K63 chain formation. The enzyme interacts with ubiquitin, and with E3 ligases of types RING, and HECT (in combination with Ube2N). Whereas K63-specific Ube2N uses a tightly bound E2-like subunit (either Ube2V1 or Ube2V2) to position the K63 side chain of the incoming (acceptor) Ub
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additional information
?
-
enzyme UBE2V1 and homologues are catalytically inactive E2-like proteins interacting with Ube2N for K63 chain formation. The enzyme interacts with ubiquitin, and with E3 ligases of types RING, and HECT (in combination with Ube2N). Whereas K63-specific Ube2N uses a tightly bound E2-like subunit (either Ube2V1 or Ube2V2) to position the K63 side chain of the incoming (acceptor) Ub
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-
additional information
?
-
enzyme UBE2V1 and homologues are catalytically inactive E2-like proteins interacting with Ube2N for K63 chain formation. The enzyme interacts with ubiquitin, and with E3 ligases of types RING, and HECT (in combination with Ube2N). Whereas K63-specific Ube2N uses a tightly bound E2-like subunit (either Ube2V1 or Ube2V2) to position the K63 side chain of the incoming (acceptor) Ub
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-
additional information
?
-
enzyme UBE2V1 and homologues are catalytically inactive E2-like proteins interacting with Ube2N for K63 chain formation. The enzyme interacts with ubiquitin, and with E3 ligases of types RING, and HECT (in combination with Ube2N). Whereas K63-specific Ube2N uses a tightly bound E2-like subunit (either Ube2V1 or Ube2V2) to position the K63 side chain of the incoming (acceptor) Ub
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-
-
additional information
?
-
enzyme UBE2V1 and homologues are catalytically inactive E2-like proteins interacting with Ube2N for K63 chain formation. The enzyme interacts with ubiquitin, and with E3 ligases of types RING, and HECT (in combination with Ube2N). Whereas K63-specific Ube2N uses a tightly bound E2-like subunit (either Ube2V1 or Ube2V2) to position the K63 side chain of the incoming (acceptor) Ub
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-
-
additional information
?
-
enzyme UBE2V1 and homologues are catalytically inactive E2-like proteins interacting with Ube2N for K63 chain formation. The enzyme interacts with ubiquitin, and with E3 ligases of types RING, and HECT (in combination with Ube2N). Whereas K63-specific Ube2N uses a tightly bound E2-like subunit (either Ube2V1 or Ube2V2) to position the K63 side chain of the incoming (acceptor) Ub
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-
-
additional information
?
-
enzyme UBE2V1 and homologues are catalytically inactive E2-like proteins interacting with Ube2N for K63 chain formation. The enzyme interacts with ubiquitin, and with E3 ligases of types RING, and HECT (in combination with Ube2N). Whereas K63-specific Ube2N uses a tightly bound E2-like subunit (either Ube2V1 or Ube2V2) to position the K63 side chain of the incoming (acceptor) Ub
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-
-
additional information
?
-
enzyme UBE2V1 and homologues are catalytically inactive E2-like proteins interacting with Ube2N for K63 chain formation. The enzyme interacts with ubiquitin, and with E3 ligases of types RING, and HECT (in combination with Ube2N). Whereas K63-specific Ube2N uses a tightly bound E2-like subunit (either Ube2V1 or Ube2V2) to position the K63 side chain of the incoming (acceptor) Ub
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-
-
additional information
?
-
enzyme UBE2V1 and homologues are catalytically inactive E2-like proteins interacting with Ube2N for K63 chain formation. The enzyme interacts with ubiquitin, and with E3 ligases of types RING, and HECT (in combination with Ube2N). Whereas K63-specific Ube2N uses a tightly bound E2-like subunit (either Ube2V1 or Ube2V2) to position the K63 side chain of the incoming (acceptor) Ub
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-
-
additional information
?
-
enzyme UBE2V1 and homologues are catalytically inactive E2-like proteins interacting with Ube2N for K63 chain formation. The enzyme interacts with ubiquitin, and with E3 ligases of types RING, and HECT (in combination with Ube2N). Whereas K63-specific Ube2N uses a tightly bound E2-like subunit (either Ube2V1 or Ube2V2) to position the K63 side chain of the incoming (acceptor) Ub
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-
-
additional information
?
-
enzyme UBE2V1 and homologues are catalytically inactive E2-like proteins interacting with Ube2N for K63 chain formation. The enzyme interacts with ubiquitin, and with E3 ligases of types RING, and HECT (in combination with Ube2N). Whereas K63-specific Ube2N uses a tightly bound E2-like subunit (either Ube2V1 or Ube2V2) to position the K63 side chain of the incoming (acceptor) Ub
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-
-
additional information
?
-
enzyme UBE2V1 and homologues are catalytically inactive E2-like proteins interacting with Ube2N for K63 chain formation. The enzyme interacts with ubiquitin, and with E3 ligases of types RING, and HECT (in combination with Ube2N). Whereas K63-specific Ube2N uses a tightly bound E2-like subunit (either Ube2V1 or Ube2V2) to position the K63 side chain of the incoming (acceptor) Ub
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-
-
additional information
?
-
enzyme UBE2V1 and homologues are catalytically inactive E2-like proteins interacting with Ube2N for K63 chain formation. The enzyme interacts with ubiquitin, and with E3 ligases of types RING, and HECT (in combination with Ube2N). Whereas K63-specific Ube2N uses a tightly bound E2-like subunit (either Ube2V1 or Ube2V2) to position the K63 side chain of the incoming (acceptor) Ub
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-
-
additional information
?
-
enzyme UBE2V1 and homologues are catalytically inactive E2-like proteins interacting with Ube2N for K63 chain formation. The enzyme interacts with ubiquitin, and with E3 ligases of types RING, and HECT (in combination with Ube2N). Whereas K63-specific Ube2N uses a tightly bound E2-like subunit (either Ube2V1 or Ube2V2) to position the K63 side chain of the incoming (acceptor) Ub
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-
-
additional information
?
-
enzyme UBE2V1 and homologues are catalytically inactive E2-like proteins interacting with Ube2N for K63 chain formation. The enzyme interacts with ubiquitin, and with E3 ligases of types RING, and HECT (in combination with Ube2N). Whereas K63-specific Ube2N uses a tightly bound E2-like subunit (either Ube2V1 or Ube2V2) to position the K63 side chain of the incoming (acceptor) Ub
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-
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additional information
?
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enzyme UBE2V1 and homologues are catalytically inactive E2-like proteins interacting with Ube2N for K63 chain formation. The enzyme interacts with ubiquitin, and with E3 ligases of types RING, and HECT (in combination with Ube2N). Whereas K63-specific Ube2N uses a tightly bound E2-like subunit (either Ube2V1 or Ube2V2) to position the K63 side chain of the incoming (acceptor) Ub
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-
-
additional information
?
-
enzyme UBE2V1 and homologues are catalytically inactive E2-like proteins interacting with Ube2N for K63 chain formation. The enzyme interacts with ubiquitin, and with E3 ligases of types RING, and HECT (in combination with Ube2N). Whereas K63-specific Ube2N uses a tightly bound E2-like subunit (either Ube2V1 or Ube2V2) to position the K63 side chain of the incoming (acceptor) Ub
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-
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additional information
?
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enzyme UBE2V1 and homologues are catalytically inactive E2-like proteins interacting with Ube2N for K63 chain formation. The enzyme interacts with ubiquitin, and with E3 ligases of types RING, and HECT (in combination with Ube2N). Whereas K63-specific Ube2N uses a tightly bound E2-like subunit (either Ube2V1 or Ube2V2) to position the K63 side chain of the incoming (acceptor) Ub
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additional information
?
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enzyme UBE2V1 and homologues are catalytically inactive E2-like proteins interacting with Ube2N for K63 chain formation. The enzyme interacts with ubiquitin, and with E3 ligases of types RING, and HECT (in combination with Ube2N). Whereas K63-specific Ube2N uses a tightly bound E2-like subunit (either Ube2V1 or Ube2V2) to position the K63 side chain of the incoming (acceptor) Ub
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additional information
?
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the enzyme interacts with E3 ligase of type RING
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additional information
?
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the enzyme interacts with E3 ligase of type RING
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additional information
?
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the enzyme interacts with E3 ligase of type RING
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additional information
?
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the enzyme interacts with E3 ligase of type RING
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additional information
?
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the enzyme interacts with E3 ligase of type RING
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additional information
?
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the enzyme interacts with E3 ligase of type RING
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additional information
?
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the enzyme interacts with E3 ligase of type RING
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additional information
?
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the enzyme interacts with E3 ligase of type RING
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additional information
?
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the enzyme interacts with E3 ligase of type RING
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additional information
?
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the enzyme interacts with E3 ligase of type RING
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additional information
?
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the enzyme interacts with E3 ligase of type RING
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additional information
?
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the enzyme interacts with E3 ligase of type RING
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additional information
?
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the enzyme interacts with E3 ligase of type RING
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additional information
?
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the enzyme interacts with E3 ligase of type RING
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additional information
?
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the enzyme interacts with E3 ligase of type RING
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additional information
?
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the enzyme interacts with E3 ligase of type RING
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additional information
?
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the enzyme interacts with E3 ligase of type RING
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additional information
?
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the enzyme interacts with E3 ligase of type RING
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additional information
?
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the enzyme interacts with E3 ligase of type RING
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additional information
?
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the enzyme interacts with E3 ligase of type RING
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additional information
?
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the enzyme interacts with E3 ligase of type RING
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additional information
?
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the enzyme interacts with E3 ligase of type RING
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additional information
?
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the enzyme interacts with E3 ligase of type RING
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additional information
?
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the enzyme interacts with E3 ligase of type RING
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additional information
?
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the enzyme interacts with E3 ligase of type RING
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additional information
?
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the enzyme interacts with E3 ligase of type RING
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additional information
?
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the enzyme interacts with E3 ligase of type RING
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additional information
?
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the enzyme interacts with E3 ligase of type RING
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additional information
?
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the enzyme interacts with E3 ligase of type RING
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additional information
?
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the enzyme interacts with E3 ligase of type RING
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additional information
?
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the enzyme interacts with E3 ligases of types HECT, and RBR, but not with E3 RING, and not with ubiquitin. UBE2L3 is a cysteine-only reactive E2
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additional information
?
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the enzyme interacts with E3 ligases of types HECT, and RBR, but not with E3 RING, and not with ubiquitin. UBE2L3 is a cysteine-only reactive E2
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additional information
?
-
the enzyme interacts with E3 ligases of types HECT, and RBR, but not with E3 RING, and not with ubiquitin. UBE2L3 is a cysteine-only reactive E2
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additional information
?
-
the enzyme interacts with E3 ligases of types HECT, and RBR, but not with E3 RING, and not with ubiquitin. UBE2L3 is a cysteine-only reactive E2
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additional information
?
-
the enzyme interacts with E3 ligases of types HECT, and RBR, but not with E3 RING, and not with ubiquitin. UBE2L3 is a cysteine-only reactive E2
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additional information
?
-
the enzyme interacts with E3 ligases of types HECT, and RBR, but not with E3 RING, and not with ubiquitin. UBE2L3 is a cysteine-only reactive E2
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additional information
?
-
the enzyme interacts with E3 ligases of types HECT, and RBR, but not with E3 RING, and not with ubiquitin. UBE2L3 is a cysteine-only reactive E2
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additional information
?
-
the enzyme interacts with E3 ligases of types HECT, and RBR, but not with E3 RING, and not with ubiquitin. UBE2L3 is a cysteine-only reactive E2
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additional information
?
-
the enzyme interacts with E3 ligases of types HECT, and RBR, but not with E3 RING, and not with ubiquitin. UBE2L3 is a cysteine-only reactive E2
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additional information
?
-
the enzyme interacts with E3 ligases of types HECT, and RBR, but not with E3 RING, and not with ubiquitin. UBE2L3 is a cysteine-only reactive E2
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additional information
?
-
the enzyme interacts with E3 ligases of types HECT, and RBR, but not with E3 RING, and not with ubiquitin. UBE2L3 is a cysteine-only reactive E2
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additional information
?
-
the enzyme interacts with E3 ligases of types HECT, and RBR, but not with E3 RING, and not with ubiquitin. UBE2L3 is a cysteine-only reactive E2
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additional information
?
-
the enzyme interacts with E3 ligases of types HECT, and RBR, but not with E3 RING, and not with ubiquitin. UBE2L3 is a cysteine-only reactive E2
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-
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additional information
?
-
the enzyme interacts with E3 ligases of types HECT, and RBR, but not with E3 RING, and not with ubiquitin. UBE2L3 is a cysteine-only reactive E2
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additional information
?
-
the enzyme interacts with E3 ligases of types HECT, and RBR, but not with E3 RING, and not with ubiquitin. UBE2L3 is a cysteine-only reactive E2
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-
-
additional information
?
-
the enzyme interacts with E3 ligases of types HECT, and RBR, but not with E3 RING, and not with ubiquitin. UBE2L3 is a cysteine-only reactive E2
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additional information
?
-
the enzyme interacts with E3 ligases of types HECT, and RBR, but not with E3 RING, and not with ubiquitin. UBE2L3 is a cysteine-only reactive E2
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-
-
additional information
?
-
the enzyme interacts with E3 ligases of types HECT, and RBR, but not with E3 RING, and not with ubiquitin. UBE2L3 is a cysteine-only reactive E2
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-
-
additional information
?
-
the enzyme interacts with E3 ligases of types HECT, and RBR, but not with E3 RING, and not with ubiquitin. UBE2L3 is a cysteine-only reactive E2
-
-
-
additional information
?
-
the enzyme interacts with E3 ligases of types HECT, and RBR, but not with E3 RING, and not with ubiquitin. UBE2L3 is a cysteine-only reactive E2
-
-
-
additional information
?
-
the enzyme interacts with E3 ligases of types HECT, and RBR, but not with E3 RING, and not with ubiquitin. UBE2L3 is a cysteine-only reactive E2
-
-
-
additional information
?
-
the enzyme interacts with E3 ligases of types HECT, and RBR, but not with E3 RING, and not with ubiquitin. UBE2L3 is a cysteine-only reactive E2
-
-
-
additional information
?
-
the enzyme interacts with E3 ligases of types HECT, and RBR, but not with E3 RING, and not with ubiquitin. UBE2L3 is a cysteine-only reactive E2
-
-
-
additional information
?
-
the enzyme interacts with E3 ligases of types HECT, and RBR, but not with E3 RING, and not with ubiquitin. UBE2L3 is a cysteine-only reactive E2
-
-
-
additional information
?
-
the enzyme interacts with E3 ligases of types HECT, and RBR, but not with E3 RING, and not with ubiquitin. UBE2L3 is a cysteine-only reactive E2
-
-
-
additional information
?
-
the enzyme interacts with E3 ligases of types HECT, and RBR, but not with E3 RING, and not with ubiquitin. UBE2L3 is a cysteine-only reactive E2
-
-
-
additional information
?
-
the enzyme interacts with E3 ligases of types HECT, and RBR, but not with E3 RING, and not with ubiquitin. UBE2L3 is a cysteine-only reactive E2
-
-
-
additional information
?
-
the enzyme interacts with E3 ligases of types HECT, and RBR, but not with E3 RING, and not with ubiquitin. UBE2L3 is a cysteine-only reactive E2
-
-
-
additional information
?
-
the enzyme interacts with E3 ligases of types HECT, and RBR, but not with E3 RING, and not with ubiquitin. UBE2L3 is a cysteine-only reactive E2
-
-
-
additional information
?
-
the enzyme interacts with E3 ligases of types HECT, and RBR, but not with E3 RING, and not with ubiquitin. UBE2L3 is a cysteine-only reactive E2
-
-
-
additional information
?
-
the enzyme interacts with E3 ligases of types HECT, RBR, and RING, but not with ubiquitin. UBE2N builds K63 Ub-chains, inetracts with UBE2V1 and UBE2V2 for K63 chain formation. K63-specific Ube2N uses a tightly bound E2-like subunit (either Ube2V1 or Ube2V2) to position the K63 side chain of the incoming (acceptor) Ub. A substrate that is modified by Ube2W (EC 2.3.2.25) can serve as the template for chain building by Ube2N and Ube2K. K63-linked polyUb is built directly onto the active site cysteine of Ube2N
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additional information
?
-
the enzyme interacts with E3 ligases of types HECT, RBR, and RING, but not with ubiquitin. UBE2N builds K63 Ub-chains, inetracts with UBE2V1 and UBE2V2 for K63 chain formation. K63-specific Ube2N uses a tightly bound E2-like subunit (either Ube2V1 or Ube2V2) to position the K63 side chain of the incoming (acceptor) Ub. A substrate that is modified by Ube2W (EC 2.3.2.25) can serve as the template for chain building by Ube2N and Ube2K. K63-linked polyUb is built directly onto the active site cysteine of Ube2N
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-
-
additional information
?
-
the enzyme interacts with E3 ligases of types HECT, RBR, and RING, but not with ubiquitin. UBE2N builds K63 Ub-chains, inetracts with UBE2V1 and UBE2V2 for K63 chain formation. K63-specific Ube2N uses a tightly bound E2-like subunit (either Ube2V1 or Ube2V2) to position the K63 side chain of the incoming (acceptor) Ub. A substrate that is modified by Ube2W (EC 2.3.2.25) can serve as the template for chain building by Ube2N and Ube2K. K63-linked polyUb is built directly onto the active site cysteine of Ube2N
-
-
-
additional information
?
-
the enzyme interacts with E3 ligases of types HECT, RBR, and RING, but not with ubiquitin. UBE2N builds K63 Ub-chains, inetracts with UBE2V1 and UBE2V2 for K63 chain formation. K63-specific Ube2N uses a tightly bound E2-like subunit (either Ube2V1 or Ube2V2) to position the K63 side chain of the incoming (acceptor) Ub. A substrate that is modified by Ube2W (EC 2.3.2.25) can serve as the template for chain building by Ube2N and Ube2K. K63-linked polyUb is built directly onto the active site cysteine of Ube2N
-
-
-
additional information
?
-
the enzyme interacts with E3 ligases of types HECT, RBR, and RING, but not with ubiquitin. UBE2N builds K63 Ub-chains, inetracts with UBE2V1 and UBE2V2 for K63 chain formation. K63-specific Ube2N uses a tightly bound E2-like subunit (either Ube2V1 or Ube2V2) to position the K63 side chain of the incoming (acceptor) Ub. A substrate that is modified by Ube2W (EC 2.3.2.25) can serve as the template for chain building by Ube2N and Ube2K. K63-linked polyUb is built directly onto the active site cysteine of Ube2N
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-
-
additional information
?
-
the enzyme interacts with E3 ligases of types HECT, RBR, and RING, but not with ubiquitin. UBE2N builds K63 Ub-chains, inetracts with UBE2V1 and UBE2V2 for K63 chain formation. K63-specific Ube2N uses a tightly bound E2-like subunit (either Ube2V1 or Ube2V2) to position the K63 side chain of the incoming (acceptor) Ub. A substrate that is modified by Ube2W (EC 2.3.2.25) can serve as the template for chain building by Ube2N and Ube2K. K63-linked polyUb is built directly onto the active site cysteine of Ube2N
-
-
-
additional information
?
-
the enzyme interacts with E3 ligases of types HECT, RBR, and RING, but not with ubiquitin. UBE2N builds K63 Ub-chains, inetracts with UBE2V1 and UBE2V2 for K63 chain formation. K63-specific Ube2N uses a tightly bound E2-like subunit (either Ube2V1 or Ube2V2) to position the K63 side chain of the incoming (acceptor) Ub. A substrate that is modified by Ube2W (EC 2.3.2.25) can serve as the template for chain building by Ube2N and Ube2K. K63-linked polyUb is built directly onto the active site cysteine of Ube2N
-
-
-
additional information
?
-
the enzyme interacts with E3 ligases of types HECT, RBR, and RING, but not with ubiquitin. UBE2N builds K63 Ub-chains, inetracts with UBE2V1 and UBE2V2 for K63 chain formation. K63-specific Ube2N uses a tightly bound E2-like subunit (either Ube2V1 or Ube2V2) to position the K63 side chain of the incoming (acceptor) Ub. A substrate that is modified by Ube2W (EC 2.3.2.25) can serve as the template for chain building by Ube2N and Ube2K. K63-linked polyUb is built directly onto the active site cysteine of Ube2N
-
-
-
additional information
?
-
the enzyme interacts with E3 ligases of types HECT, RBR, and RING, but not with ubiquitin. UBE2N builds K63 Ub-chains, inetracts with UBE2V1 and UBE2V2 for K63 chain formation. K63-specific Ube2N uses a tightly bound E2-like subunit (either Ube2V1 or Ube2V2) to position the K63 side chain of the incoming (acceptor) Ub. A substrate that is modified by Ube2W (EC 2.3.2.25) can serve as the template for chain building by Ube2N and Ube2K. K63-linked polyUb is built directly onto the active site cysteine of Ube2N
-
-
-
additional information
?
-
the enzyme interacts with E3 ligases of types HECT, RBR, and RING, but not with ubiquitin. UBE2N builds K63 Ub-chains, inetracts with UBE2V1 and UBE2V2 for K63 chain formation. K63-specific Ube2N uses a tightly bound E2-like subunit (either Ube2V1 or Ube2V2) to position the K63 side chain of the incoming (acceptor) Ub. A substrate that is modified by Ube2W (EC 2.3.2.25) can serve as the template for chain building by Ube2N and Ube2K. K63-linked polyUb is built directly onto the active site cysteine of Ube2N
-
-
-
additional information
?
-
the enzyme interacts with E3 ligases of types HECT, RBR, and RING, but not with ubiquitin. UBE2N builds K63 Ub-chains, inetracts with UBE2V1 and UBE2V2 for K63 chain formation. K63-specific Ube2N uses a tightly bound E2-like subunit (either Ube2V1 or Ube2V2) to position the K63 side chain of the incoming (acceptor) Ub. A substrate that is modified by Ube2W (EC 2.3.2.25) can serve as the template for chain building by Ube2N and Ube2K. K63-linked polyUb is built directly onto the active site cysteine of Ube2N
-
-
-
additional information
?
-
the enzyme interacts with E3 ligases of types HECT, RBR, and RING, but not with ubiquitin. UBE2N builds K63 Ub-chains, inetracts with UBE2V1 and UBE2V2 for K63 chain formation. K63-specific Ube2N uses a tightly bound E2-like subunit (either Ube2V1 or Ube2V2) to position the K63 side chain of the incoming (acceptor) Ub. A substrate that is modified by Ube2W (EC 2.3.2.25) can serve as the template for chain building by Ube2N and Ube2K. K63-linked polyUb is built directly onto the active site cysteine of Ube2N
-
-
-
additional information
?
-
the enzyme interacts with E3 ligases of types HECT, RBR, and RING, but not with ubiquitin. UBE2N builds K63 Ub-chains, inetracts with UBE2V1 and UBE2V2 for K63 chain formation. K63-specific Ube2N uses a tightly bound E2-like subunit (either Ube2V1 or Ube2V2) to position the K63 side chain of the incoming (acceptor) Ub. A substrate that is modified by Ube2W (EC 2.3.2.25) can serve as the template for chain building by Ube2N and Ube2K. K63-linked polyUb is built directly onto the active site cysteine of Ube2N
-
-
-
additional information
?
-
the enzyme interacts with E3 ligases of types HECT, RBR, and RING, but not with ubiquitin. UBE2N builds K63 Ub-chains, inetracts with UBE2V1 and UBE2V2 for K63 chain formation. K63-specific Ube2N uses a tightly bound E2-like subunit (either Ube2V1 or Ube2V2) to position the K63 side chain of the incoming (acceptor) Ub. A substrate that is modified by Ube2W (EC 2.3.2.25) can serve as the template for chain building by Ube2N and Ube2K. K63-linked polyUb is built directly onto the active site cysteine of Ube2N
-
-
-
additional information
?
-
the enzyme interacts with E3 ligases of types HECT, RBR, and RING, but not with ubiquitin. UBE2N builds K63 Ub-chains, inetracts with UBE2V1 and UBE2V2 for K63 chain formation. K63-specific Ube2N uses a tightly bound E2-like subunit (either Ube2V1 or Ube2V2) to position the K63 side chain of the incoming (acceptor) Ub. A substrate that is modified by Ube2W (EC 2.3.2.25) can serve as the template for chain building by Ube2N and Ube2K. K63-linked polyUb is built directly onto the active site cysteine of Ube2N
-
-
-
additional information
?
-
the enzyme interacts with E3 ligases of types HECT, RBR, and RING, but not with ubiquitin. UBE2N builds K63 Ub-chains, inetracts with UBE2V1 and UBE2V2 for K63 chain formation. K63-specific Ube2N uses a tightly bound E2-like subunit (either Ube2V1 or Ube2V2) to position the K63 side chain of the incoming (acceptor) Ub. A substrate that is modified by Ube2W (EC 2.3.2.25) can serve as the template for chain building by Ube2N and Ube2K. K63-linked polyUb is built directly onto the active site cysteine of Ube2N
-
-
-
additional information
?
-
the enzyme interacts with E3 ligases of types HECT, RBR, and RING, but not with ubiquitin. UBE2N builds K63 Ub-chains, inetracts with UBE2V1 and UBE2V2 for K63 chain formation. K63-specific Ube2N uses a tightly bound E2-like subunit (either Ube2V1 or Ube2V2) to position the K63 side chain of the incoming (acceptor) Ub. A substrate that is modified by Ube2W (EC 2.3.2.25) can serve as the template for chain building by Ube2N and Ube2K. K63-linked polyUb is built directly onto the active site cysteine of Ube2N
-
-
-
additional information
?
-
the enzyme interacts with E3 ligases of types HECT, RBR, and RING, but not with ubiquitin. UBE2N builds K63 Ub-chains, inetracts with UBE2V1 and UBE2V2 for K63 chain formation. K63-specific Ube2N uses a tightly bound E2-like subunit (either Ube2V1 or Ube2V2) to position the K63 side chain of the incoming (acceptor) Ub. A substrate that is modified by Ube2W (EC 2.3.2.25) can serve as the template for chain building by Ube2N and Ube2K. K63-linked polyUb is built directly onto the active site cysteine of Ube2N
-
-
-
additional information
?
-
the enzyme interacts with E3 ligases of types HECT, RBR, and RING, but not with ubiquitin. UBE2N builds K63 Ub-chains, inetracts with UBE2V1 and UBE2V2 for K63 chain formation. K63-specific Ube2N uses a tightly bound E2-like subunit (either Ube2V1 or Ube2V2) to position the K63 side chain of the incoming (acceptor) Ub. A substrate that is modified by Ube2W (EC 2.3.2.25) can serve as the template for chain building by Ube2N and Ube2K. K63-linked polyUb is built directly onto the active site cysteine of Ube2N
-
-
-
additional information
?
-
the enzyme interacts with E3 ligases of types HECT, RBR, and RING, but not with ubiquitin. UBE2N builds K63 Ub-chains, inetracts with UBE2V1 and UBE2V2 for K63 chain formation. K63-specific Ube2N uses a tightly bound E2-like subunit (either Ube2V1 or Ube2V2) to position the K63 side chain of the incoming (acceptor) Ub. A substrate that is modified by Ube2W (EC 2.3.2.25) can serve as the template for chain building by Ube2N and Ube2K. K63-linked polyUb is built directly onto the active site cysteine of Ube2N
-
-
-
additional information
?
-
the enzyme interacts with E3 ligases of types HECT, RBR, and RING, but not with ubiquitin. UBE2N builds K63 Ub-chains, inetracts with UBE2V1 and UBE2V2 for K63 chain formation. K63-specific Ube2N uses a tightly bound E2-like subunit (either Ube2V1 or Ube2V2) to position the K63 side chain of the incoming (acceptor) Ub. A substrate that is modified by Ube2W (EC 2.3.2.25) can serve as the template for chain building by Ube2N and Ube2K. K63-linked polyUb is built directly onto the active site cysteine of Ube2N
-
-
-
additional information
?
-
the enzyme interacts with E3 ligases of types HECT, RBR, and RING, but not with ubiquitin. UBE2N builds K63 Ub-chains, inetracts with UBE2V1 and UBE2V2 for K63 chain formation. K63-specific Ube2N uses a tightly bound E2-like subunit (either Ube2V1 or Ube2V2) to position the K63 side chain of the incoming (acceptor) Ub. A substrate that is modified by Ube2W (EC 2.3.2.25) can serve as the template for chain building by Ube2N and Ube2K. K63-linked polyUb is built directly onto the active site cysteine of Ube2N
-
-
-
additional information
?
-
the enzyme interacts with E3 ligases of types HECT, RBR, and RING, but not with ubiquitin. UBE2N builds K63 Ub-chains, inetracts with UBE2V1 and UBE2V2 for K63 chain formation. K63-specific Ube2N uses a tightly bound E2-like subunit (either Ube2V1 or Ube2V2) to position the K63 side chain of the incoming (acceptor) Ub. A substrate that is modified by Ube2W (EC 2.3.2.25) can serve as the template for chain building by Ube2N and Ube2K. K63-linked polyUb is built directly onto the active site cysteine of Ube2N
-
-
-
additional information
?
-
the enzyme interacts with E3 ligases of types HECT, RBR, and RING, but not with ubiquitin. UBE2N builds K63 Ub-chains, inetracts with UBE2V1 and UBE2V2 for K63 chain formation. K63-specific Ube2N uses a tightly bound E2-like subunit (either Ube2V1 or Ube2V2) to position the K63 side chain of the incoming (acceptor) Ub. A substrate that is modified by Ube2W (EC 2.3.2.25) can serve as the template for chain building by Ube2N and Ube2K. K63-linked polyUb is built directly onto the active site cysteine of Ube2N
-
-
-
additional information
?
-
the enzyme interacts with E3 ligases of types HECT, RBR, and RING, but not with ubiquitin. UBE2N builds K63 Ub-chains, inetracts with UBE2V1 and UBE2V2 for K63 chain formation. K63-specific Ube2N uses a tightly bound E2-like subunit (either Ube2V1 or Ube2V2) to position the K63 side chain of the incoming (acceptor) Ub. A substrate that is modified by Ube2W (EC 2.3.2.25) can serve as the template for chain building by Ube2N and Ube2K. K63-linked polyUb is built directly onto the active site cysteine of Ube2N
-
-
-
additional information
?
-
the enzyme interacts with E3 ligases of types HECT, RBR, and RING, but not with ubiquitin. UBE2N builds K63 Ub-chains, inetracts with UBE2V1 and UBE2V2 for K63 chain formation. K63-specific Ube2N uses a tightly bound E2-like subunit (either Ube2V1 or Ube2V2) to position the K63 side chain of the incoming (acceptor) Ub. A substrate that is modified by Ube2W (EC 2.3.2.25) can serve as the template for chain building by Ube2N and Ube2K. K63-linked polyUb is built directly onto the active site cysteine of Ube2N
-
-
-
additional information
?
-
the enzyme interacts with E3 ligases of types HECT, RBR, and RING, but not with ubiquitin. UBE2N builds K63 Ub-chains, inetracts with UBE2V1 and UBE2V2 for K63 chain formation. K63-specific Ube2N uses a tightly bound E2-like subunit (either Ube2V1 or Ube2V2) to position the K63 side chain of the incoming (acceptor) Ub. A substrate that is modified by Ube2W (EC 2.3.2.25) can serve as the template for chain building by Ube2N and Ube2K. K63-linked polyUb is built directly onto the active site cysteine of Ube2N
-
-
-
additional information
?
-
the enzyme interacts with E3 ligases of types HECT, RBR, and RING, but not with ubiquitin. UBE2N builds K63 Ub-chains, inetracts with UBE2V1 and UBE2V2 for K63 chain formation. K63-specific Ube2N uses a tightly bound E2-like subunit (either Ube2V1 or Ube2V2) to position the K63 side chain of the incoming (acceptor) Ub. A substrate that is modified by Ube2W (EC 2.3.2.25) can serve as the template for chain building by Ube2N and Ube2K. K63-linked polyUb is built directly onto the active site cysteine of Ube2N
-
-
-
additional information
?
-
the enzyme interacts with E3 ligases of types HECT, RBR, and RING, but not with ubiquitin. UBE2N builds K63 Ub-chains, inetracts with UBE2V1 and UBE2V2 for K63 chain formation. K63-specific Ube2N uses a tightly bound E2-like subunit (either Ube2V1 or Ube2V2) to position the K63 side chain of the incoming (acceptor) Ub. A substrate that is modified by Ube2W (EC 2.3.2.25) can serve as the template for chain building by Ube2N and Ube2K. K63-linked polyUb is built directly onto the active site cysteine of Ube2N
-
-
-
additional information
?
-
the enzyme interacts with E3 ligases of types HECT, RBR, and RING, but not with ubiquitin. UBE2N builds K63 Ub-chains, inetracts with UBE2V1 and UBE2V2 for K63 chain formation. K63-specific Ube2N uses a tightly bound E2-like subunit (either Ube2V1 or Ube2V2) to position the K63 side chain of the incoming (acceptor) Ub. A substrate that is modified by Ube2W (EC 2.3.2.25) can serve as the template for chain building by Ube2N and Ube2K. K63-linked polyUb is built directly onto the active site cysteine of Ube2N
-
-
-
additional information
?
-
the enzyme interacts with E3 ligases of types RING and HECT
-
-
-
additional information
?
-
the enzyme interacts with E3 ligases of types RING and HECT
-
-
-
additional information
?
-
the enzyme interacts with E3 ligases of types RING and HECT
-
-
-
additional information
?
-
the enzyme interacts with E3 ligases of types RING and HECT
-
-
-
additional information
?
-
the enzyme interacts with E3 ligases of types RING and HECT
-
-
-
additional information
?
-
the enzyme interacts with E3 ligases of types RING and HECT
-
-
-
additional information
?
-
the enzyme interacts with E3 ligases of types RING and HECT
-
-
-
additional information
?
-
the enzyme interacts with E3 ligases of types RING and HECT
-
-
-
additional information
?
-
the enzyme interacts with E3 ligases of types RING and HECT
-
-
-
additional information
?
-
the enzyme interacts with E3 ligases of types RING and HECT
-
-
-
additional information
?
-
the enzyme interacts with E3 ligases of types RING and HECT
-
-
-
additional information
?
-
the enzyme interacts with E3 ligases of types RING and HECT
-
-
-
additional information
?
-
the enzyme interacts with E3 ligases of types RING and HECT
-
-
-
additional information
?
-
the enzyme interacts with E3 ligases of types RING and HECT
-
-
-
additional information
?
-
the enzyme interacts with E3 ligases of types RING and HECT
-
-
-
additional information
?
-
the enzyme interacts with E3 ligases of types RING and HECT
-
-
-
additional information
?
-
the enzyme interacts with E3 ligases of types RING and HECT
-
-
-
additional information
?
-
the enzyme interacts with E3 ligases of types RING and HECT
-
-
-
additional information
?
-
the enzyme interacts with E3 ligases of types RING and HECT
-
-
-
additional information
?
-
the enzyme interacts with E3 ligases of types RING and HECT
-
-
-
additional information
?
-
the enzyme interacts with E3 ligases of types RING and HECT
-
-
-
additional information
?
-
the enzyme interacts with E3 ligases of types RING and HECT
-
-
-
additional information
?
-
the enzyme interacts with E3 ligases of types RING and HECT
-
-
-
additional information
?
-
the enzyme interacts with E3 ligases of types RING and HECT
-
-
-
additional information
?
-
the enzyme interacts with E3 ligases of types RING and HECT
-
-
-
additional information
?
-
the enzyme interacts with E3 ligases of types RING and HECT
-
-
-
additional information
?
-
the enzyme interacts with E3 ligases of types RING and HECT
-
-
-
additional information
?
-
the enzyme interacts with E3 ligases of types RING and HECT
-
-
-
additional information
?
-
the enzyme interacts with E3 ligases of types RING and HECT
-
-
-
additional information
?
-
the enzyme interacts with E3 ligases of types RING and HECT
-
-
-
additional information
?
-
the enzyme interacts with E3 ligases of types RING and HECT. UBE2G1 is a K48 chain-building enzyme even in the absence of an E3
-
-
-
additional information
?
-
the enzyme interacts with E3 ligases of types RING and HECT. UBE2G1 is a K48 chain-building enzyme even in the absence of an E3
-
-
-
additional information
?
-
the enzyme interacts with E3 ligases of types RING and HECT. UBE2G1 is a K48 chain-building enzyme even in the absence of an E3
-
-
-
additional information
?
-
the enzyme interacts with E3 ligases of types RING and HECT. UBE2G1 is a K48 chain-building enzyme even in the absence of an E3
-
-
-
additional information
?
-
the enzyme interacts with E3 ligases of types RING and HECT. UBE2G1 is a K48 chain-building enzyme even in the absence of an E3
-
-
-
additional information
?
-
the enzyme interacts with E3 ligases of types RING and HECT. UBE2G1 is a K48 chain-building enzyme even in the absence of an E3
-
-
-
additional information
?
-
the enzyme interacts with E3 ligases of types RING and HECT. UBE2G1 is a K48 chain-building enzyme even in the absence of an E3
-
-
-
additional information
?
-
the enzyme interacts with E3 ligases of types RING and HECT. UBE2G1 is a K48 chain-building enzyme even in the absence of an E3
-
-
-
additional information
?
-
the enzyme interacts with E3 ligases of types RING and HECT. UBE2G1 is a K48 chain-building enzyme even in the absence of an E3
-
-
-
additional information
?
-
the enzyme interacts with E3 ligases of types RING and HECT. UBE2G1 is a K48 chain-building enzyme even in the absence of an E3
-
-
-
additional information
?
-
the enzyme interacts with E3 ligases of types RING and HECT. UBE2G1 is a K48 chain-building enzyme even in the absence of an E3
-
-
-
additional information
?
-
the enzyme interacts with E3 ligases of types RING and HECT. UBE2G1 is a K48 chain-building enzyme even in the absence of an E3
-
-
-
additional information
?
-
the enzyme interacts with E3 ligases of types RING and HECT. UBE2G1 is a K48 chain-building enzyme even in the absence of an E3
-
-
-
additional information
?
-
the enzyme interacts with E3 ligases of types RING and HECT. UBE2G1 is a K48 chain-building enzyme even in the absence of an E3
-
-
-
additional information
?
-
the enzyme interacts with E3 ligases of types RING and HECT. UBE2G1 is a K48 chain-building enzyme even in the absence of an E3
-
-
-
additional information
?
-
the enzyme interacts with E3 ligases of types RING and HECT. UBE2G1 is a K48 chain-building enzyme even in the absence of an E3
-
-
-
additional information
?
-
the enzyme interacts with E3 ligases of types RING and HECT. UBE2G1 is a K48 chain-building enzyme even in the absence of an E3
-
-
-
additional information
?
-
the enzyme interacts with E3 ligases of types RING and HECT. UBE2G1 is a K48 chain-building enzyme even in the absence of an E3
-
-
-
additional information
?
-
the enzyme interacts with E3 ligases of types RING and HECT. UBE2G1 is a K48 chain-building enzyme even in the absence of an E3
-
-
-
additional information
?
-
the enzyme interacts with E3 ligases of types RING and HECT. UBE2G1 is a K48 chain-building enzyme even in the absence of an E3
-
-
-
additional information
?
-
the enzyme interacts with E3 ligases of types RING and HECT. UBE2G1 is a K48 chain-building enzyme even in the absence of an E3
-
-
-
additional information
?
-
the enzyme interacts with E3 ligases of types RING and HECT. UBE2G1 is a K48 chain-building enzyme even in the absence of an E3
-
-
-
additional information
?
-
the enzyme interacts with E3 ligases of types RING and HECT. UBE2G1 is a K48 chain-building enzyme even in the absence of an E3
-
-
-
additional information
?
-
the enzyme interacts with E3 ligases of types RING and HECT. UBE2G1 is a K48 chain-building enzyme even in the absence of an E3
-
-
-
additional information
?
-
the enzyme interacts with E3 ligases of types RING and HECT. UBE2G1 is a K48 chain-building enzyme even in the absence of an E3
-
-
-
additional information
?
-
the enzyme interacts with E3 ligases of types RING and HECT. UBE2G1 is a K48 chain-building enzyme even in the absence of an E3
-
-
-
additional information
?
-
the enzyme interacts with E3 ligases of types RING and HECT. UBE2G1 is a K48 chain-building enzyme even in the absence of an E3
-
-
-
additional information
?
-
the enzyme interacts with E3 ligases of types RING and HECT. UBE2G1 is a K48 chain-building enzyme even in the absence of an E3
-
-
-
additional information
?
-
the enzyme interacts with E3 ligases of types RING and HECT. UBE2G1 is a K48 chain-building enzyme even in the absence of an E3
-
-
-
additional information
?
-
the enzyme interacts with E3 ligases of types RING and HECT. UBE2G1 is a K48 chain-building enzyme even in the absence of an E3
-
-
-
additional information
?
-
the enzyme interacts with E3 ligases of types RING, and RBR. Ube2L6 is a bispecific E2 active with ISG15 and ubiquitin (Ub)
-
-
-
additional information
?
-
the enzyme interacts with E3 ligases of types RING, and RBR. Ube2L6 is a bispecific E2 active with ISG15 and ubiquitin (Ub)
-
-
-
additional information
?
-
the enzyme interacts with E3 ligases of types RING, and RBR. Ube2L6 is a bispecific E2 active with ISG15 and ubiquitin (Ub)
-
-
-
additional information
?
-
the enzyme interacts with E3 ligases of types RING, and RBR. Ube2L6 is a bispecific E2 active with ISG15 and ubiquitin (Ub)
-
-
-
additional information
?
-
the enzyme interacts with E3 ligases of types RING, and RBR. Ube2L6 is a bispecific E2 active with ISG15 and ubiquitin (Ub)
-
-
-
additional information
?
-
the enzyme interacts with E3 ligases of types RING, and RBR. Ube2L6 is a bispecific E2 active with ISG15 and ubiquitin (Ub)
-
-
-
additional information
?
-
the enzyme interacts with E3 ligases of types RING, and RBR. Ube2L6 is a bispecific E2 active with ISG15 and ubiquitin (Ub)
-
-
-
additional information
?
-
the enzyme interacts with E3 ligases of types RING, and RBR. Ube2L6 is a bispecific E2 active with ISG15 and ubiquitin (Ub)
-
-
-
additional information
?
-
the enzyme interacts with E3 ligases of types RING, and RBR. Ube2L6 is a bispecific E2 active with ISG15 and ubiquitin (Ub)
-
-
-
additional information
?
-
the enzyme interacts with E3 ligases of types RING, and RBR. Ube2L6 is a bispecific E2 active with ISG15 and ubiquitin (Ub)
-
-
-
additional information
?
-
the enzyme interacts with E3 ligases of types RING, and RBR. Ube2L6 is a bispecific E2 active with ISG15 and ubiquitin (Ub)
-
-
-
additional information
?
-
the enzyme interacts with E3 ligases of types RING, and RBR. Ube2L6 is a bispecific E2 active with ISG15 and ubiquitin (Ub)
-
-
-
additional information
?
-
the enzyme interacts with E3 ligases of types RING, and RBR. Ube2L6 is a bispecific E2 active with ISG15 and ubiquitin (Ub)
-
-
-
additional information
?
-
the enzyme interacts with E3 ligases of types RING, and RBR. Ube2L6 is a bispecific E2 active with ISG15 and ubiquitin (Ub)
-
-
-
additional information
?
-
the enzyme interacts with E3 ligases of types RING, and RBR. Ube2L6 is a bispecific E2 active with ISG15 and ubiquitin (Ub)
-
-
-
additional information
?
-
the enzyme interacts with E3 ligases of types RING, and RBR. Ube2L6 is a bispecific E2 active with ISG15 and ubiquitin (Ub)
-
-
-
additional information
?
-
the enzyme interacts with E3 ligases of types RING, and RBR. Ube2L6 is a bispecific E2 active with ISG15 and ubiquitin (Ub)
-
-
-
additional information
?
-
the enzyme interacts with E3 ligases of types RING, and RBR. Ube2L6 is a bispecific E2 active with ISG15 and ubiquitin (Ub)
-
-
-
additional information
?
-
the enzyme interacts with E3 ligases of types RING, and RBR. Ube2L6 is a bispecific E2 active with ISG15 and ubiquitin (Ub)
-
-
-
additional information
?
-
the enzyme interacts with E3 ligases of types RING, and RBR. Ube2L6 is a bispecific E2 active with ISG15 and ubiquitin (Ub)
-
-
-
additional information
?
-
the enzyme interacts with E3 ligases of types RING, and RBR. Ube2L6 is a bispecific E2 active with ISG15 and ubiquitin (Ub)
-
-
-
additional information
?
-
the enzyme interacts with E3 ligases of types RING, and RBR. Ube2L6 is a bispecific E2 active with ISG15 and ubiquitin (Ub)
-
-
-
additional information
?
-
the enzyme interacts with E3 ligases of types RING, and RBR. Ube2L6 is a bispecific E2 active with ISG15 and ubiquitin (Ub)
-
-
-
additional information
?
-
the enzyme interacts with E3 ligases of types RING, and RBR. Ube2L6 is a bispecific E2 active with ISG15 and ubiquitin (Ub)
-
-
-
additional information
?
-
the enzyme interacts with E3 ligases of types RING, and RBR. Ube2L6 is a bispecific E2 active with ISG15 and ubiquitin (Ub)
-
-
-
additional information
?
-
the enzyme interacts with E3 ligases of types RING, and RBR. Ube2L6 is a bispecific E2 active with ISG15 and ubiquitin (Ub)
-
-
-
additional information
?
-
the enzyme interacts with E3 ligases of types RING, and RBR. Ube2L6 is a bispecific E2 active with ISG15 and ubiquitin (Ub)
-
-
-
additional information
?
-
the enzyme interacts with E3 ligases of types RING, and RBR. Ube2L6 is a bispecific E2 active with ISG15 and ubiquitin (Ub)
-
-
-
additional information
?
-
the enzyme interacts with E3 ligases of types RING, and RBR. Ube2L6 is a bispecific E2 active with ISG15 and ubiquitin (Ub)
-
-
-
additional information
?
-
the enzyme interacts with E3 ligases of types RING, and RBR. Ube2L6 is a bispecific E2 active with ISG15 and ubiquitin (Ub)
-
-
-
additional information
?
-
the enzyme interacts with E3 ligases of types RING, HECT, and RBR
-
-
-
additional information
?
-
the enzyme interacts with E3 ligases of types RING, HECT, and RBR
-
-
-
additional information
?
-
the enzyme interacts with E3 ligases of types RING, HECT, and RBR
-
-
-
additional information
?
-
the enzyme interacts with E3 ligases of types RING, HECT, and RBR
-
-
-
additional information
?
-
the enzyme interacts with E3 ligases of types RING, HECT, and RBR
-
-
-
additional information
?
-
the enzyme interacts with E3 ligases of types RING, HECT, and RBR
-
-
-
additional information
?
-
the enzyme interacts with E3 ligases of types RING, HECT, and RBR
-
-
-
additional information
?
-
the enzyme interacts with E3 ligases of types RING, HECT, and RBR
-
-
-
additional information
?
-
the enzyme interacts with E3 ligases of types RING, HECT, and RBR
-
-
-
additional information
?
-
the enzyme interacts with E3 ligases of types RING, HECT, and RBR
-
-
-
additional information
?
-
the enzyme interacts with E3 ligases of types RING, HECT, and RBR
-
-
-
additional information
?
-
the enzyme interacts with E3 ligases of types RING, HECT, and RBR
-
-
-
additional information
?
-
the enzyme interacts with E3 ligases of types RING, HECT, and RBR
-
-
-
additional information
?
-
the enzyme interacts with E3 ligases of types RING, HECT, and RBR
-
-
-
additional information
?
-
the enzyme interacts with E3 ligases of types RING, HECT, and RBR
-
-
-
additional information
?
-
the enzyme interacts with E3 ligases of types RING, HECT, and RBR
-
-
-
additional information
?
-
the enzyme interacts with E3 ligases of types RING, HECT, and RBR
-
-
-
additional information
?
-
the enzyme interacts with E3 ligases of types RING, HECT, and RBR
-
-
-
additional information
?
-
the enzyme interacts with E3 ligases of types RING, HECT, and RBR
-
-
-
additional information
?
-
the enzyme interacts with E3 ligases of types RING, HECT, and RBR
-
-
-
additional information
?
-
the enzyme interacts with E3 ligases of types RING, HECT, and RBR
-
-
-
additional information
?
-
the enzyme interacts with E3 ligases of types RING, HECT, and RBR
-
-
-
additional information
?
-
the enzyme interacts with E3 ligases of types RING, HECT, and RBR
-
-
-
additional information
?
-
the enzyme interacts with E3 ligases of types RING, HECT, and RBR
-
-
-
additional information
?
-
the enzyme interacts with E3 ligases of types RING, HECT, and RBR
-
-
-
additional information
?
-
the enzyme interacts with E3 ligases of types RING, HECT, and RBR
-
-
-
additional information
?
-
the enzyme interacts with E3 ligases of types RING, HECT, and RBR
-
-
-
additional information
?
-
the enzyme interacts with E3 ligases of types RING, HECT, and RBR
-
-
-
additional information
?
-
the enzyme interacts with E3 ligases of types RING, HECT, and RBR
-
-
-
additional information
?
-
the enzyme interacts with E3 ligases of types RING, HECT, and RBR
-
-
-
additional information
?
-
the enzyme interacts with E3 ligases of types RING, HECT, and RBR, but not with ubiquitin
-
-
-
additional information
?
-
the enzyme interacts with E3 ligases of types RING, HECT, and RBR, but not with ubiquitin
-
-
-
additional information
?
-
the enzyme interacts with E3 ligases of types RING, HECT, and RBR, but not with ubiquitin
-
-
-
additional information
?
-
the enzyme interacts with E3 ligases of types RING, HECT, and RBR, but not with ubiquitin
-
-
-
additional information
?
-
the enzyme interacts with E3 ligases of types RING, HECT, and RBR, but not with ubiquitin
-
-
-
additional information
?
-
the enzyme interacts with E3 ligases of types RING, HECT, and RBR, but not with ubiquitin
-
-
-
additional information
?
-
the enzyme interacts with E3 ligases of types RING, HECT, and RBR, but not with ubiquitin
-
-
-
additional information
?
-
the enzyme interacts with E3 ligases of types RING, HECT, and RBR, but not with ubiquitin
-
-
-
additional information
?
-
the enzyme interacts with E3 ligases of types RING, HECT, and RBR, but not with ubiquitin
-
-
-
additional information
?
-
the enzyme interacts with E3 ligases of types RING, HECT, and RBR, but not with ubiquitin
-
-
-
additional information
?
-
the enzyme interacts with E3 ligases of types RING, HECT, and RBR, but not with ubiquitin
-
-
-
additional information
?
-
the enzyme interacts with E3 ligases of types RING, HECT, and RBR, but not with ubiquitin
-
-
-
additional information
?
-
the enzyme interacts with E3 ligases of types RING, HECT, and RBR, but not with ubiquitin
-
-
-
additional information
?
-
the enzyme interacts with E3 ligases of types RING, HECT, and RBR, but not with ubiquitin
-
-
-
additional information
?
-
the enzyme interacts with E3 ligases of types RING, HECT, and RBR, but not with ubiquitin
-
-
-
additional information
?
-
the enzyme interacts with E3 ligases of types RING, HECT, and RBR, but not with ubiquitin
-
-
-
additional information
?
-
the enzyme interacts with E3 ligases of types RING, HECT, and RBR, but not with ubiquitin
-
-
-
additional information
?
-
the enzyme interacts with E3 ligases of types RING, HECT, and RBR, but not with ubiquitin
-
-
-
additional information
?
-
the enzyme interacts with E3 ligases of types RING, HECT, and RBR, but not with ubiquitin
-
-
-
additional information
?
-
the enzyme interacts with E3 ligases of types RING, HECT, and RBR, but not with ubiquitin
-
-
-
additional information
?
-
the enzyme interacts with E3 ligases of types RING, HECT, and RBR, but not with ubiquitin
-
-
-
additional information
?
-
the enzyme interacts with E3 ligases of types RING, HECT, and RBR, but not with ubiquitin
-
-
-
additional information
?
-
the enzyme interacts with E3 ligases of types RING, HECT, and RBR, but not with ubiquitin
-
-
-
additional information
?
-
the enzyme interacts with E3 ligases of types RING, HECT, and RBR, but not with ubiquitin
-
-
-
additional information
?
-
the enzyme interacts with E3 ligases of types RING, HECT, and RBR, but not with ubiquitin
-
-
-
additional information
?
-
the enzyme interacts with E3 ligases of types RING, HECT, and RBR, but not with ubiquitin
-
-
-
additional information
?
-
the enzyme interacts with E3 ligases of types RING, HECT, and RBR, but not with ubiquitin
-
-
-
additional information
?
-
the enzyme interacts with E3 ligases of types RING, HECT, and RBR, but not with ubiquitin
-
-
-
additional information
?
-
the enzyme interacts with E3 ligases of types RING, HECT, and RBR, but not with ubiquitin
-
-
-
additional information
?
-
the enzyme interacts with E3 ligases of types RING, HECT, and RBR, but not with ubiquitin
-
-
-
additional information
?
-
the enzyme interacts with E3 ligases of types RING, HECT, and RBR, but not with ubiquitin. Ube2E1 provides an example of E2 regulation by autoubiquitylation. Modification occurs on a lysine near the active site and on lysines in the unstructured N-terminal extension of Ube2E1
-
-
-
additional information
?
-
the enzyme interacts with E3 ligases of types RING, HECT, and RBR, but not with ubiquitin. Ube2E1 provides an example of E2 regulation by autoubiquitylation. Modification occurs on a lysine near the active site and on lysines in the unstructured N-terminal extension of Ube2E1
-
-
-
additional information
?
-
the enzyme interacts with E3 ligases of types RING, HECT, and RBR, but not with ubiquitin. Ube2E1 provides an example of E2 regulation by autoubiquitylation. Modification occurs on a lysine near the active site and on lysines in the unstructured N-terminal extension of Ube2E1
-
-
-
additional information
?
-
the enzyme interacts with E3 ligases of types RING, HECT, and RBR, but not with ubiquitin. Ube2E1 provides an example of E2 regulation by autoubiquitylation. Modification occurs on a lysine near the active site and on lysines in the unstructured N-terminal extension of Ube2E1
-
-
-
additional information
?
-
the enzyme interacts with E3 ligases of types RING, HECT, and RBR, but not with ubiquitin. Ube2E1 provides an example of E2 regulation by autoubiquitylation. Modification occurs on a lysine near the active site and on lysines in the unstructured N-terminal extension of Ube2E1
-
-
-
additional information
?
-
the enzyme interacts with E3 ligases of types RING, HECT, and RBR, but not with ubiquitin. Ube2E1 provides an example of E2 regulation by autoubiquitylation. Modification occurs on a lysine near the active site and on lysines in the unstructured N-terminal extension of Ube2E1
-
-
-
additional information
?
-
the enzyme interacts with E3 ligases of types RING, HECT, and RBR, but not with ubiquitin. Ube2E1 provides an example of E2 regulation by autoubiquitylation. Modification occurs on a lysine near the active site and on lysines in the unstructured N-terminal extension of Ube2E1
-
-
-
additional information
?
-
the enzyme interacts with E3 ligases of types RING, HECT, and RBR, but not with ubiquitin. Ube2E1 provides an example of E2 regulation by autoubiquitylation. Modification occurs on a lysine near the active site and on lysines in the unstructured N-terminal extension of Ube2E1
-
-
-
additional information
?
-
the enzyme interacts with E3 ligases of types RING, HECT, and RBR, but not with ubiquitin. Ube2E1 provides an example of E2 regulation by autoubiquitylation. Modification occurs on a lysine near the active site and on lysines in the unstructured N-terminal extension of Ube2E1
-
-
-
additional information
?
-
the enzyme interacts with E3 ligases of types RING, HECT, and RBR, but not with ubiquitin. Ube2E1 provides an example of E2 regulation by autoubiquitylation. Modification occurs on a lysine near the active site and on lysines in the unstructured N-terminal extension of Ube2E1
-
-
-
additional information
?
-
the enzyme interacts with E3 ligases of types RING, HECT, and RBR, but not with ubiquitin. Ube2E1 provides an example of E2 regulation by autoubiquitylation. Modification occurs on a lysine near the active site and on lysines in the unstructured N-terminal extension of Ube2E1
-
-
-
additional information
?
-
the enzyme interacts with E3 ligases of types RING, HECT, and RBR, but not with ubiquitin. Ube2E1 provides an example of E2 regulation by autoubiquitylation. Modification occurs on a lysine near the active site and on lysines in the unstructured N-terminal extension of Ube2E1
-
-
-
additional information
?
-
the enzyme interacts with E3 ligases of types RING, HECT, and RBR, but not with ubiquitin. Ube2E1 provides an example of E2 regulation by autoubiquitylation. Modification occurs on a lysine near the active site and on lysines in the unstructured N-terminal extension of Ube2E1
-
-
-
additional information
?
-
the enzyme interacts with E3 ligases of types RING, HECT, and RBR, but not with ubiquitin. Ube2E1 provides an example of E2 regulation by autoubiquitylation. Modification occurs on a lysine near the active site and on lysines in the unstructured N-terminal extension of Ube2E1
-
-
-
additional information
?
-
the enzyme interacts with E3 ligases of types RING, HECT, and RBR, but not with ubiquitin. Ube2E1 provides an example of E2 regulation by autoubiquitylation. Modification occurs on a lysine near the active site and on lysines in the unstructured N-terminal extension of Ube2E1
-
-
-
additional information
?
-
the enzyme interacts with E3 ligases of types RING, HECT, and RBR, but not with ubiquitin. Ube2E1 provides an example of E2 regulation by autoubiquitylation. Modification occurs on a lysine near the active site and on lysines in the unstructured N-terminal extension of Ube2E1
-
-
-
additional information
?
-
the enzyme interacts with E3 ligases of types RING, HECT, and RBR, but not with ubiquitin. Ube2E1 provides an example of E2 regulation by autoubiquitylation. Modification occurs on a lysine near the active site and on lysines in the unstructured N-terminal extension of Ube2E1
-
-
-
additional information
?
-
the enzyme interacts with E3 ligases of types RING, HECT, and RBR, but not with ubiquitin. Ube2E1 provides an example of E2 regulation by autoubiquitylation. Modification occurs on a lysine near the active site and on lysines in the unstructured N-terminal extension of Ube2E1
-
-
-
additional information
?
-
the enzyme interacts with E3 ligases of types RING, HECT, and RBR, but not with ubiquitin. Ube2E1 provides an example of E2 regulation by autoubiquitylation. Modification occurs on a lysine near the active site and on lysines in the unstructured N-terminal extension of Ube2E1
-
-
-
additional information
?
-
the enzyme interacts with E3 ligases of types RING, HECT, and RBR, but not with ubiquitin. Ube2E1 provides an example of E2 regulation by autoubiquitylation. Modification occurs on a lysine near the active site and on lysines in the unstructured N-terminal extension of Ube2E1
-
-
-
additional information
?
-
the enzyme interacts with E3 ligases of types RING, HECT, and RBR, but not with ubiquitin. Ube2E1 provides an example of E2 regulation by autoubiquitylation. Modification occurs on a lysine near the active site and on lysines in the unstructured N-terminal extension of Ube2E1
-
-
-
additional information
?
-
the enzyme interacts with E3 ligases of types RING, HECT, and RBR, but not with ubiquitin. Ube2E1 provides an example of E2 regulation by autoubiquitylation. Modification occurs on a lysine near the active site and on lysines in the unstructured N-terminal extension of Ube2E1
-
-
-
additional information
?
-
the enzyme interacts with E3 ligases of types RING, HECT, and RBR, but not with ubiquitin. Ube2E1 provides an example of E2 regulation by autoubiquitylation. Modification occurs on a lysine near the active site and on lysines in the unstructured N-terminal extension of Ube2E1
-
-
-
additional information
?
-
the enzyme interacts with E3 ligases of types RING, HECT, and RBR, but not with ubiquitin. Ube2E1 provides an example of E2 regulation by autoubiquitylation. Modification occurs on a lysine near the active site and on lysines in the unstructured N-terminal extension of Ube2E1
-
-
-
additional information
?
-
the enzyme interacts with E3 ligases of types RING, HECT, and RBR, but not with ubiquitin. Ube2E1 provides an example of E2 regulation by autoubiquitylation. Modification occurs on a lysine near the active site and on lysines in the unstructured N-terminal extension of Ube2E1
-
-
-
additional information
?
-
the enzyme interacts with E3 ligases of types RING, HECT, and RBR, but not with ubiquitin. Ube2E1 provides an example of E2 regulation by autoubiquitylation. Modification occurs on a lysine near the active site and on lysines in the unstructured N-terminal extension of Ube2E1
-
-
-
additional information
?
-
the enzyme interacts with E3 ligases of types RING, HECT, and RBR, but not with ubiquitin. Ube2E1 provides an example of E2 regulation by autoubiquitylation. Modification occurs on a lysine near the active site and on lysines in the unstructured N-terminal extension of Ube2E1
-
-
-
additional information
?
-
the enzyme interacts with E3 ligases of types RING, HECT, and RBR, but not with ubiquitin. Ube2E1 provides an example of E2 regulation by autoubiquitylation. Modification occurs on a lysine near the active site and on lysines in the unstructured N-terminal extension of Ube2E1
-
-
-
additional information
?
-
the enzyme interacts with E3 ligases of types RING, HECT, and RBR, but not with ubiquitin. Ube2E1 provides an example of E2 regulation by autoubiquitylation. Modification occurs on a lysine near the active site and on lysines in the unstructured N-terminal extension of Ube2E1
-
-
-
additional information
?
-
the enzyme interacts with E3 ligases of types RING, HECT, and RBR, but not with ubiquitin. Ube2E1 provides an example of E2 regulation by autoubiquitylation. Modification occurs on a lysine near the active site and on lysines in the unstructured N-terminal extension of Ube2E1
-
-
-
additional information
?
-
the enzyme interacts with E3 ligases of types RING, HECT, and RBR. It is K48 chain-building enzyme even in the absence of an E3. Ube2K has a unique region near its active site that interacts with a tyrosine near K48 in the acceptor Ub to provide K48-linkage specificity
-
-
-
additional information
?
-
the enzyme interacts with E3 ligases of types RING, HECT, and RBR. It is K48 chain-building enzyme even in the absence of an E3. Ube2K has a unique region near its active site that interacts with a tyrosine near K48 in the acceptor Ub to provide K48-linkage specificity
-
-
-
additional information
?
-
the enzyme interacts with E3 ligases of types RING, HECT, and RBR. It is K48 chain-building enzyme even in the absence of an E3. Ube2K has a unique region near its active site that interacts with a tyrosine near K48 in the acceptor Ub to provide K48-linkage specificity
-
-
-
additional information
?
-
the enzyme interacts with E3 ligases of types RING, HECT, and RBR. It is K48 chain-building enzyme even in the absence of an E3. Ube2K has a unique region near its active site that interacts with a tyrosine near K48 in the acceptor Ub to provide K48-linkage specificity
-
-
-
additional information
?
-
the enzyme interacts with E3 ligases of types RING, HECT, and RBR. It is K48 chain-building enzyme even in the absence of an E3. Ube2K has a unique region near its active site that interacts with a tyrosine near K48 in the acceptor Ub to provide K48-linkage specificity
-
-
-
additional information
?
-
the enzyme interacts with E3 ligases of types RING, HECT, and RBR. It is K48 chain-building enzyme even in the absence of an E3. Ube2K has a unique region near its active site that interacts with a tyrosine near K48 in the acceptor Ub to provide K48-linkage specificity
-
-
-
additional information
?
-
the enzyme interacts with E3 ligases of types RING, HECT, and RBR. It is K48 chain-building enzyme even in the absence of an E3. Ube2K has a unique region near its active site that interacts with a tyrosine near K48 in the acceptor Ub to provide K48-linkage specificity
-
-
-
additional information
?
-
the enzyme interacts with E3 ligases of types RING, HECT, and RBR. It is K48 chain-building enzyme even in the absence of an E3. Ube2K has a unique region near its active site that interacts with a tyrosine near K48 in the acceptor Ub to provide K48-linkage specificity
-
-
-
additional information
?
-
the enzyme interacts with E3 ligases of types RING, HECT, and RBR. It is K48 chain-building enzyme even in the absence of an E3. Ube2K has a unique region near its active site that interacts with a tyrosine near K48 in the acceptor Ub to provide K48-linkage specificity
-
-
-
additional information
?
-
the enzyme interacts with E3 ligases of types RING, HECT, and RBR. It is K48 chain-building enzyme even in the absence of an E3. Ube2K has a unique region near its active site that interacts with a tyrosine near K48 in the acceptor Ub to provide K48-linkage specificity
-
-
-
additional information
?
-
the enzyme interacts with E3 ligases of types RING, HECT, and RBR. It is K48 chain-building enzyme even in the absence of an E3. Ube2K has a unique region near its active site that interacts with a tyrosine near K48 in the acceptor Ub to provide K48-linkage specificity
-
-
-
additional information
?
-
the enzyme interacts with E3 ligases of types RING, HECT, and RBR. It is K48 chain-building enzyme even in the absence of an E3. Ube2K has a unique region near its active site that interacts with a tyrosine near K48 in the acceptor Ub to provide K48-linkage specificity
-
-
-
additional information
?
-
the enzyme interacts with E3 ligases of types RING, HECT, and RBR. It is K48 chain-building enzyme even in the absence of an E3. Ube2K has a unique region near its active site that interacts with a tyrosine near K48 in the acceptor Ub to provide K48-linkage specificity
-
-
-
additional information
?
-
the enzyme interacts with E3 ligases of types RING, HECT, and RBR. It is K48 chain-building enzyme even in the absence of an E3. Ube2K has a unique region near its active site that interacts with a tyrosine near K48 in the acceptor Ub to provide K48-linkage specificity
-
-
-
additional information
?
-
the enzyme interacts with E3 ligases of types RING, HECT, and RBR. It is K48 chain-building enzyme even in the absence of an E3. Ube2K has a unique region near its active site that interacts with a tyrosine near K48 in the acceptor Ub to provide K48-linkage specificity
-
-
-
additional information
?
-
the enzyme interacts with E3 ligases of types RING, HECT, and RBR. It is K48 chain-building enzyme even in the absence of an E3. Ube2K has a unique region near its active site that interacts with a tyrosine near K48 in the acceptor Ub to provide K48-linkage specificity
-
-
-
additional information
?
-
the enzyme interacts with E3 ligases of types RING, HECT, and RBR. It is K48 chain-building enzyme even in the absence of an E3. Ube2K has a unique region near its active site that interacts with a tyrosine near K48 in the acceptor Ub to provide K48-linkage specificity
-
-
-
additional information
?
-
the enzyme interacts with E3 ligases of types RING, HECT, and RBR. It is K48 chain-building enzyme even in the absence of an E3. Ube2K has a unique region near its active site that interacts with a tyrosine near K48 in the acceptor Ub to provide K48-linkage specificity
-
-
-
additional information
?
-
the enzyme interacts with E3 ligases of types RING, HECT, and RBR. It is K48 chain-building enzyme even in the absence of an E3. Ube2K has a unique region near its active site that interacts with a tyrosine near K48 in the acceptor Ub to provide K48-linkage specificity
-
-
-
additional information
?
-
the enzyme interacts with E3 ligases of types RING, HECT, and RBR. It is K48 chain-building enzyme even in the absence of an E3. Ube2K has a unique region near its active site that interacts with a tyrosine near K48 in the acceptor Ub to provide K48-linkage specificity
-
-
-
additional information
?
-
the enzyme interacts with E3 ligases of types RING, HECT, and RBR. It is K48 chain-building enzyme even in the absence of an E3. Ube2K has a unique region near its active site that interacts with a tyrosine near K48 in the acceptor Ub to provide K48-linkage specificity
-
-
-
additional information
?
-
the enzyme interacts with E3 ligases of types RING, HECT, and RBR. It is K48 chain-building enzyme even in the absence of an E3. Ube2K has a unique region near its active site that interacts with a tyrosine near K48 in the acceptor Ub to provide K48-linkage specificity
-
-
-
additional information
?
-
the enzyme interacts with E3 ligases of types RING, HECT, and RBR. It is K48 chain-building enzyme even in the absence of an E3. Ube2K has a unique region near its active site that interacts with a tyrosine near K48 in the acceptor Ub to provide K48-linkage specificity
-
-
-
additional information
?
-
the enzyme interacts with E3 ligases of types RING, HECT, and RBR. It is K48 chain-building enzyme even in the absence of an E3. Ube2K has a unique region near its active site that interacts with a tyrosine near K48 in the acceptor Ub to provide K48-linkage specificity
-
-
-
additional information
?
-
the enzyme interacts with E3 ligases of types RING, HECT, and RBR. It is K48 chain-building enzyme even in the absence of an E3. Ube2K has a unique region near its active site that interacts with a tyrosine near K48 in the acceptor Ub to provide K48-linkage specificity
-
-
-
additional information
?
-
the enzyme interacts with E3 ligases of types RING, HECT, and RBR. It is K48 chain-building enzyme even in the absence of an E3. Ube2K has a unique region near its active site that interacts with a tyrosine near K48 in the acceptor Ub to provide K48-linkage specificity
-
-
-
additional information
?
-
the enzyme interacts with E3 ligases of types RING, HECT, and RBR. It is K48 chain-building enzyme even in the absence of an E3. Ube2K has a unique region near its active site that interacts with a tyrosine near K48 in the acceptor Ub to provide K48-linkage specificity
-
-
-
additional information
?
-
the enzyme interacts with E3 ligases of types RING, HECT, and RBR. It is K48 chain-building enzyme even in the absence of an E3. Ube2K has a unique region near its active site that interacts with a tyrosine near K48 in the acceptor Ub to provide K48-linkage specificity
-
-
-
additional information
?
-
the enzyme interacts with E3 ligases of types RING, HECT, and RBR. It is K48 chain-building enzyme even in the absence of an E3. Ube2K has a unique region near its active site that interacts with a tyrosine near K48 in the acceptor Ub to provide K48-linkage specificity
-
-
-
additional information
?
-
the enzyme interacts with E3 ligases of types RING, HECT, and RBR. It is K48 chain-building enzyme even in the absence of an E3. Ube2K has a unique region near its active site that interacts with a tyrosine near K48 in the acceptor Ub to provide K48-linkage specificity
-
-
-
additional information
?
-
the enzyme interacts with E3 ligases of types RING, HECT, and RBR. Its shows hydroxyl specificity (serine/threonine)
-
-
-
additional information
?
-
the enzyme interacts with E3 ligases of types RING, HECT, and RBR. Its shows hydroxyl specificity (serine/threonine)
-
-
-
additional information
?
-
the enzyme interacts with E3 ligases of types RING, HECT, and RBR. Its shows hydroxyl specificity (serine/threonine)
-
-
-
additional information
?
-
the enzyme interacts with E3 ligases of types RING, HECT, and RBR. Its shows hydroxyl specificity (serine/threonine)
-
-
-
additional information
?
-
the enzyme interacts with E3 ligases of types RING, HECT, and RBR. Its shows hydroxyl specificity (serine/threonine)
-
-
-
additional information
?
-
the enzyme interacts with E3 ligases of types RING, HECT, and RBR. Its shows hydroxyl specificity (serine/threonine)
-
-
-
additional information
?
-
the enzyme interacts with E3 ligases of types RING, HECT, and RBR. Its shows hydroxyl specificity (serine/threonine)
-
-
-
additional information
?
-
the enzyme interacts with E3 ligases of types RING, HECT, and RBR. Its shows hydroxyl specificity (serine/threonine)
-
-
-
additional information
?
-
the enzyme interacts with E3 ligases of types RING, HECT, and RBR. Its shows hydroxyl specificity (serine/threonine)
-
-
-
additional information
?
-
the enzyme interacts with E3 ligases of types RING, HECT, and RBR. Its shows hydroxyl specificity (serine/threonine)
-
-
-
additional information
?
-
the enzyme interacts with E3 ligases of types RING, HECT, and RBR. Its shows hydroxyl specificity (serine/threonine)
-
-
-
additional information
?
-
the enzyme interacts with E3 ligases of types RING, HECT, and RBR. Its shows hydroxyl specificity (serine/threonine)
-
-
-
additional information
?
-
the enzyme interacts with E3 ligases of types RING, HECT, and RBR. Its shows hydroxyl specificity (serine/threonine)
-
-
-
additional information
?
-
the enzyme interacts with E3 ligases of types RING, HECT, and RBR. Its shows hydroxyl specificity (serine/threonine)
-
-
-
additional information
?
-
the enzyme interacts with E3 ligases of types RING, HECT, and RBR. Its shows hydroxyl specificity (serine/threonine)
-
-
-
additional information
?
-
the enzyme interacts with E3 ligases of types RING, HECT, and RBR. Its shows hydroxyl specificity (serine/threonine)
-
-
-
additional information
?
-
the enzyme interacts with E3 ligases of types RING, HECT, and RBR. Its shows hydroxyl specificity (serine/threonine)
-
-
-
additional information
?
-
the enzyme interacts with E3 ligases of types RING, HECT, and RBR. Its shows hydroxyl specificity (serine/threonine)
-
-
-
additional information
?
-
the enzyme interacts with E3 ligases of types RING, HECT, and RBR. Its shows hydroxyl specificity (serine/threonine)
-
-
-
additional information
?
-
the enzyme interacts with E3 ligases of types RING, HECT, and RBR. Its shows hydroxyl specificity (serine/threonine)
-
-
-
additional information
?
-
the enzyme interacts with E3 ligases of types RING, HECT, and RBR. Its shows hydroxyl specificity (serine/threonine)
-
-
-
additional information
?
-
the enzyme interacts with E3 ligases of types RING, HECT, and RBR. Its shows hydroxyl specificity (serine/threonine)
-
-
-
additional information
?
-
the enzyme interacts with E3 ligases of types RING, HECT, and RBR. Its shows hydroxyl specificity (serine/threonine)
-
-
-
additional information
?
-
the enzyme interacts with E3 ligases of types RING, HECT, and RBR. Its shows hydroxyl specificity (serine/threonine)
-
-
-
additional information
?
-
the enzyme interacts with E3 ligases of types RING, HECT, and RBR. Its shows hydroxyl specificity (serine/threonine)
-
-
-
additional information
?
-
the enzyme interacts with E3 ligases of types RING, HECT, and RBR. Its shows hydroxyl specificity (serine/threonine)
-
-
-
additional information
?
-
the enzyme interacts with E3 ligases of types RING, HECT, and RBR. Its shows hydroxyl specificity (serine/threonine)
-
-
-
additional information
?
-
the enzyme interacts with E3 ligases of types RING, HECT, and RBR. Its shows hydroxyl specificity (serine/threonine)
-
-
-
additional information
?
-
the enzyme interacts with E3 ligases of types RING, HECT, and RBR. Its shows hydroxyl specificity (serine/threonine)
-
-
-
additional information
?
-
the enzyme interacts with E3 ligases of types RING, HECT, and RBR. Its shows hydroxyl specificity (serine/threonine)
-
-
-
additional information
?
-
the enzyme interacts with E3 ligases of types RING, HECT, and RBR. Ube2R1 is a K48 Ub chain-building enzyme. Ube2R1 is the cognate E2 of SCF E3 ligases. K48-specific Ube2R2 has a short about 12 amino acid insertion proximal to the E2 active site that determines specificity. The highly specific chain builders such as Ube2N, Ube2S, and Ube2R1 can only transfer their conjugated Ub to another Ub molecule
-
-
-
additional information
?
-
the enzyme interacts with E3 ligases of types RING, HECT, and RBR. Ube2R1 is a K48 Ub chain-building enzyme. Ube2R1 is the cognate E2 of SCF E3 ligases. K48-specific Ube2R2 has a short about 12 amino acid insertion proximal to the E2 active site that determines specificity. The highly specific chain builders such as Ube2N, Ube2S, and Ube2R1 can only transfer their conjugated Ub to another Ub molecule
-
-
-
additional information
?
-
the enzyme interacts with E3 ligases of types RING, HECT, and RBR. Ube2R1 is a K48 Ub chain-building enzyme. Ube2R1 is the cognate E2 of SCF E3 ligases. K48-specific Ube2R2 has a short about 12 amino acid insertion proximal to the E2 active site that determines specificity. The highly specific chain builders such as Ube2N, Ube2S, and Ube2R1 can only transfer their conjugated Ub to another Ub molecule
-
-
-
additional information
?
-
the enzyme interacts with E3 ligases of types RING, HECT, and RBR. Ube2R1 is a K48 Ub chain-building enzyme. Ube2R1 is the cognate E2 of SCF E3 ligases. K48-specific Ube2R2 has a short about 12 amino acid insertion proximal to the E2 active site that determines specificity. The highly specific chain builders such as Ube2N, Ube2S, and Ube2R1 can only transfer their conjugated Ub to another Ub molecule
-
-
-
additional information
?
-
the enzyme interacts with E3 ligases of types RING, HECT, and RBR. Ube2R1 is a K48 Ub chain-building enzyme. Ube2R1 is the cognate E2 of SCF E3 ligases. K48-specific Ube2R2 has a short about 12 amino acid insertion proximal to the E2 active site that determines specificity. The highly specific chain builders such as Ube2N, Ube2S, and Ube2R1 can only transfer their conjugated Ub to another Ub molecule
-
-
-
additional information
?
-
the enzyme interacts with E3 ligases of types RING, HECT, and RBR. Ube2R1 is a K48 Ub chain-building enzyme. Ube2R1 is the cognate E2 of SCF E3 ligases. K48-specific Ube2R2 has a short about 12 amino acid insertion proximal to the E2 active site that determines specificity. The highly specific chain builders such as Ube2N, Ube2S, and Ube2R1 can only transfer their conjugated Ub to another Ub molecule
-
-
-
additional information
?
-
the enzyme interacts with E3 ligases of types RING, HECT, and RBR. Ube2R1 is a K48 Ub chain-building enzyme. Ube2R1 is the cognate E2 of SCF E3 ligases. K48-specific Ube2R2 has a short about 12 amino acid insertion proximal to the E2 active site that determines specificity. The highly specific chain builders such as Ube2N, Ube2S, and Ube2R1 can only transfer their conjugated Ub to another Ub molecule
-
-
-
additional information
?
-
the enzyme interacts with E3 ligases of types RING, HECT, and RBR. Ube2R1 is a K48 Ub chain-building enzyme. Ube2R1 is the cognate E2 of SCF E3 ligases. K48-specific Ube2R2 has a short about 12 amino acid insertion proximal to the E2 active site that determines specificity. The highly specific chain builders such as Ube2N, Ube2S, and Ube2R1 can only transfer their conjugated Ub to another Ub molecule
-
-
-
additional information
?
-
the enzyme interacts with E3 ligases of types RING, HECT, and RBR. Ube2R1 is a K48 Ub chain-building enzyme. Ube2R1 is the cognate E2 of SCF E3 ligases. K48-specific Ube2R2 has a short about 12 amino acid insertion proximal to the E2 active site that determines specificity. The highly specific chain builders such as Ube2N, Ube2S, and Ube2R1 can only transfer their conjugated Ub to another Ub molecule
-
-
-
additional information
?
-
the enzyme interacts with E3 ligases of types RING, HECT, and RBR. Ube2R1 is a K48 Ub chain-building enzyme. Ube2R1 is the cognate E2 of SCF E3 ligases. K48-specific Ube2R2 has a short about 12 amino acid insertion proximal to the E2 active site that determines specificity. The highly specific chain builders such as Ube2N, Ube2S, and Ube2R1 can only transfer their conjugated Ub to another Ub molecule
-
-
-
additional information
?
-
the enzyme interacts with E3 ligases of types RING, HECT, and RBR. Ube2R1 is a K48 Ub chain-building enzyme. Ube2R1 is the cognate E2 of SCF E3 ligases. K48-specific Ube2R2 has a short about 12 amino acid insertion proximal to the E2 active site that determines specificity. The highly specific chain builders such as Ube2N, Ube2S, and Ube2R1 can only transfer their conjugated Ub to another Ub molecule
-
-
-
additional information
?
-
the enzyme interacts with E3 ligases of types RING, HECT, and RBR. Ube2R1 is a K48 Ub chain-building enzyme. Ube2R1 is the cognate E2 of SCF E3 ligases. K48-specific Ube2R2 has a short about 12 amino acid insertion proximal to the E2 active site that determines specificity. The highly specific chain builders such as Ube2N, Ube2S, and Ube2R1 can only transfer their conjugated Ub to another Ub molecule
-
-
-
additional information
?
-
the enzyme interacts with E3 ligases of types RING, HECT, and RBR. Ube2R1 is a K48 Ub chain-building enzyme. Ube2R1 is the cognate E2 of SCF E3 ligases. K48-specific Ube2R2 has a short about 12 amino acid insertion proximal to the E2 active site that determines specificity. The highly specific chain builders such as Ube2N, Ube2S, and Ube2R1 can only transfer their conjugated Ub to another Ub molecule
-
-
-
additional information
?
-
the enzyme interacts with E3 ligases of types RING, HECT, and RBR. Ube2R1 is a K48 Ub chain-building enzyme. Ube2R1 is the cognate E2 of SCF E3 ligases. K48-specific Ube2R2 has a short about 12 amino acid insertion proximal to the E2 active site that determines specificity. The highly specific chain builders such as Ube2N, Ube2S, and Ube2R1 can only transfer their conjugated Ub to another Ub molecule
-
-
-
additional information
?
-
the enzyme interacts with E3 ligases of types RING, HECT, and RBR. Ube2R1 is a K48 Ub chain-building enzyme. Ube2R1 is the cognate E2 of SCF E3 ligases. K48-specific Ube2R2 has a short about 12 amino acid insertion proximal to the E2 active site that determines specificity. The highly specific chain builders such as Ube2N, Ube2S, and Ube2R1 can only transfer their conjugated Ub to another Ub molecule
-
-
-
additional information
?
-
the enzyme interacts with E3 ligases of types RING, HECT, and RBR. Ube2R1 is a K48 Ub chain-building enzyme. Ube2R1 is the cognate E2 of SCF E3 ligases. K48-specific Ube2R2 has a short about 12 amino acid insertion proximal to the E2 active site that determines specificity. The highly specific chain builders such as Ube2N, Ube2S, and Ube2R1 can only transfer their conjugated Ub to another Ub molecule
-
-
-
additional information
?
-
the enzyme interacts with E3 ligases of types RING, HECT, and RBR. Ube2R1 is a K48 Ub chain-building enzyme. Ube2R1 is the cognate E2 of SCF E3 ligases. K48-specific Ube2R2 has a short about 12 amino acid insertion proximal to the E2 active site that determines specificity. The highly specific chain builders such as Ube2N, Ube2S, and Ube2R1 can only transfer their conjugated Ub to another Ub molecule
-
-
-
additional information
?
-
the enzyme interacts with E3 ligases of types RING, HECT, and RBR. Ube2R1 is a K48 Ub chain-building enzyme. Ube2R1 is the cognate E2 of SCF E3 ligases. K48-specific Ube2R2 has a short about 12 amino acid insertion proximal to the E2 active site that determines specificity. The highly specific chain builders such as Ube2N, Ube2S, and Ube2R1 can only transfer their conjugated Ub to another Ub molecule
-
-
-
additional information
?
-
the enzyme interacts with E3 ligases of types RING, HECT, and RBR. Ube2R1 is a K48 Ub chain-building enzyme. Ube2R1 is the cognate E2 of SCF E3 ligases. K48-specific Ube2R2 has a short about 12 amino acid insertion proximal to the E2 active site that determines specificity. The highly specific chain builders such as Ube2N, Ube2S, and Ube2R1 can only transfer their conjugated Ub to another Ub molecule
-
-
-
additional information
?
-
the enzyme interacts with E3 ligases of types RING, HECT, and RBR. Ube2R1 is a K48 Ub chain-building enzyme. Ube2R1 is the cognate E2 of SCF E3 ligases. K48-specific Ube2R2 has a short about 12 amino acid insertion proximal to the E2 active site that determines specificity. The highly specific chain builders such as Ube2N, Ube2S, and Ube2R1 can only transfer their conjugated Ub to another Ub molecule
-
-
-
additional information
?
-
the enzyme interacts with E3 ligases of types RING, HECT, and RBR. Ube2R1 is a K48 Ub chain-building enzyme. Ube2R1 is the cognate E2 of SCF E3 ligases. K48-specific Ube2R2 has a short about 12 amino acid insertion proximal to the E2 active site that determines specificity. The highly specific chain builders such as Ube2N, Ube2S, and Ube2R1 can only transfer their conjugated Ub to another Ub molecule
-
-
-
additional information
?
-
the enzyme interacts with E3 ligases of types RING, HECT, and RBR. Ube2R1 is a K48 Ub chain-building enzyme. Ube2R1 is the cognate E2 of SCF E3 ligases. K48-specific Ube2R2 has a short about 12 amino acid insertion proximal to the E2 active site that determines specificity. The highly specific chain builders such as Ube2N, Ube2S, and Ube2R1 can only transfer their conjugated Ub to another Ub molecule
-
-
-
additional information
?
-
the enzyme interacts with E3 ligases of types RING, HECT, and RBR. Ube2R1 is a K48 Ub chain-building enzyme. Ube2R1 is the cognate E2 of SCF E3 ligases. K48-specific Ube2R2 has a short about 12 amino acid insertion proximal to the E2 active site that determines specificity. The highly specific chain builders such as Ube2N, Ube2S, and Ube2R1 can only transfer their conjugated Ub to another Ub molecule
-
-
-
additional information
?
-
the enzyme interacts with E3 ligases of types RING, HECT, and RBR. Ube2R1 is a K48 Ub chain-building enzyme. Ube2R1 is the cognate E2 of SCF E3 ligases. K48-specific Ube2R2 has a short about 12 amino acid insertion proximal to the E2 active site that determines specificity. The highly specific chain builders such as Ube2N, Ube2S, and Ube2R1 can only transfer their conjugated Ub to another Ub molecule
-
-
-
additional information
?
-
the enzyme interacts with E3 ligases of types RING, HECT, and RBR. Ube2R1 is a K48 Ub chain-building enzyme. Ube2R1 is the cognate E2 of SCF E3 ligases. K48-specific Ube2R2 has a short about 12 amino acid insertion proximal to the E2 active site that determines specificity. The highly specific chain builders such as Ube2N, Ube2S, and Ube2R1 can only transfer their conjugated Ub to another Ub molecule
-
-
-
additional information
?
-
the enzyme interacts with E3 ligases of types RING, HECT, and RBR. Ube2R1 is a K48 Ub chain-building enzyme. Ube2R1 is the cognate E2 of SCF E3 ligases. K48-specific Ube2R2 has a short about 12 amino acid insertion proximal to the E2 active site that determines specificity. The highly specific chain builders such as Ube2N, Ube2S, and Ube2R1 can only transfer their conjugated Ub to another Ub molecule
-
-
-
additional information
?
-
the enzyme interacts with E3 ligases of types RING, HECT, and RBR. Ube2R1 is a K48 Ub chain-building enzyme. Ube2R1 is the cognate E2 of SCF E3 ligases. K48-specific Ube2R2 has a short about 12 amino acid insertion proximal to the E2 active site that determines specificity. The highly specific chain builders such as Ube2N, Ube2S, and Ube2R1 can only transfer their conjugated Ub to another Ub molecule
-
-
-
additional information
?
-
the enzyme interacts with E3 ligases of types RING, HECT, and RBR. Ube2R1 is a K48 Ub chain-building enzyme. Ube2R1 is the cognate E2 of SCF E3 ligases. K48-specific Ube2R2 has a short about 12 amino acid insertion proximal to the E2 active site that determines specificity. The highly specific chain builders such as Ube2N, Ube2S, and Ube2R1 can only transfer their conjugated Ub to another Ub molecule
-
-
-
additional information
?
-
the enzyme interacts with E3 ligases of types RING, HECT, and RBR. Ube2R1 is a K48 Ub chain-building enzyme. Ube2R1 is the cognate E2 of SCF E3 ligases. K48-specific Ube2R2 has a short about 12 amino acid insertion proximal to the E2 active site that determines specificity. The highly specific chain builders such as Ube2N, Ube2S, and Ube2R1 can only transfer their conjugated Ub to another Ub molecule
-
-
-
additional information
?
-
the enzyme interacts with E3 ligases of types RING, HECT, and RBR. Ube2R1 is a K48 Ub chain-building enzyme. Ube2R1 is the cognate E2 of SCF E3 ligases. K48-specific Ube2R2 has a short about 12 amino acid insertion proximal to the E2 active site that determines specificity. The highly specific chain builders such as Ube2N, Ube2S, and Ube2R1 can only transfer their conjugated Ub to another Ub molecule
-
-
-
additional information
?
-
the enzyme interacts with E3 ligases of types RING, HECT, and RBR. Ube2R2 is a K48 Ub chain-building enzyme. Ube2R1 is the cognate E2 of SCF E3 ligases. K48-specific Ube2R1 has a short about 12 amino acid insertion proximal to the E2 active site that determines specificity
-
-
-
additional information
?
-
the enzyme interacts with E3 ligases of types RING, HECT, and RBR. Ube2R2 is a K48 Ub chain-building enzyme. Ube2R1 is the cognate E2 of SCF E3 ligases. K48-specific Ube2R1 has a short about 12 amino acid insertion proximal to the E2 active site that determines specificity
-
-
-
additional information
?
-
the enzyme interacts with E3 ligases of types RING, HECT, and RBR. Ube2R2 is a K48 Ub chain-building enzyme. Ube2R1 is the cognate E2 of SCF E3 ligases. K48-specific Ube2R1 has a short about 12 amino acid insertion proximal to the E2 active site that determines specificity
-
-
-
additional information
?
-
the enzyme interacts with E3 ligases of types RING, HECT, and RBR. Ube2R2 is a K48 Ub chain-building enzyme. Ube2R1 is the cognate E2 of SCF E3 ligases. K48-specific Ube2R1 has a short about 12 amino acid insertion proximal to the E2 active site that determines specificity
-
-
-
additional information
?
-
the enzyme interacts with E3 ligases of types RING, HECT, and RBR. Ube2R2 is a K48 Ub chain-building enzyme. Ube2R1 is the cognate E2 of SCF E3 ligases. K48-specific Ube2R1 has a short about 12 amino acid insertion proximal to the E2 active site that determines specificity
-
-
-
additional information
?
-
the enzyme interacts with E3 ligases of types RING, HECT, and RBR. Ube2R2 is a K48 Ub chain-building enzyme. Ube2R1 is the cognate E2 of SCF E3 ligases. K48-specific Ube2R1 has a short about 12 amino acid insertion proximal to the E2 active site that determines specificity
-
-
-
additional information
?
-
the enzyme interacts with E3 ligases of types RING, HECT, and RBR. Ube2R2 is a K48 Ub chain-building enzyme. Ube2R1 is the cognate E2 of SCF E3 ligases. K48-specific Ube2R1 has a short about 12 amino acid insertion proximal to the E2 active site that determines specificity
-
-
-
additional information
?
-
the enzyme interacts with E3 ligases of types RING, HECT, and RBR. Ube2R2 is a K48 Ub chain-building enzyme. Ube2R1 is the cognate E2 of SCF E3 ligases. K48-specific Ube2R1 has a short about 12 amino acid insertion proximal to the E2 active site that determines specificity
-
-
-
additional information
?
-
the enzyme interacts with E3 ligases of types RING, HECT, and RBR. Ube2R2 is a K48 Ub chain-building enzyme. Ube2R1 is the cognate E2 of SCF E3 ligases. K48-specific Ube2R1 has a short about 12 amino acid insertion proximal to the E2 active site that determines specificity
-
-
-
additional information
?
-
the enzyme interacts with E3 ligases of types RING, HECT, and RBR. Ube2R2 is a K48 Ub chain-building enzyme. Ube2R1 is the cognate E2 of SCF E3 ligases. K48-specific Ube2R1 has a short about 12 amino acid insertion proximal to the E2 active site that determines specificity
-
-
-
additional information
?
-
the enzyme interacts with E3 ligases of types RING, HECT, and RBR. Ube2R2 is a K48 Ub chain-building enzyme. Ube2R1 is the cognate E2 of SCF E3 ligases. K48-specific Ube2R1 has a short about 12 amino acid insertion proximal to the E2 active site that determines specificity
-
-
-
additional information
?
-
the enzyme interacts with E3 ligases of types RING, HECT, and RBR. Ube2R2 is a K48 Ub chain-building enzyme. Ube2R1 is the cognate E2 of SCF E3 ligases. K48-specific Ube2R1 has a short about 12 amino acid insertion proximal to the E2 active site that determines specificity
-
-
-
additional information
?
-
the enzyme interacts with E3 ligases of types RING, HECT, and RBR. Ube2R2 is a K48 Ub chain-building enzyme. Ube2R1 is the cognate E2 of SCF E3 ligases. K48-specific Ube2R1 has a short about 12 amino acid insertion proximal to the E2 active site that determines specificity
-
-
-
additional information
?
-
the enzyme interacts with E3 ligases of types RING, HECT, and RBR. Ube2R2 is a K48 Ub chain-building enzyme. Ube2R1 is the cognate E2 of SCF E3 ligases. K48-specific Ube2R1 has a short about 12 amino acid insertion proximal to the E2 active site that determines specificity
-
-
-
additional information
?
-
the enzyme interacts with E3 ligases of types RING, HECT, and RBR. Ube2R2 is a K48 Ub chain-building enzyme. Ube2R1 is the cognate E2 of SCF E3 ligases. K48-specific Ube2R1 has a short about 12 amino acid insertion proximal to the E2 active site that determines specificity
-
-
-
additional information
?
-
the enzyme interacts with E3 ligases of types RING, HECT, and RBR. Ube2R2 is a K48 Ub chain-building enzyme. Ube2R1 is the cognate E2 of SCF E3 ligases. K48-specific Ube2R1 has a short about 12 amino acid insertion proximal to the E2 active site that determines specificity
-
-
-
additional information
?
-
the enzyme interacts with E3 ligases of types RING, HECT, and RBR. Ube2R2 is a K48 Ub chain-building enzyme. Ube2R1 is the cognate E2 of SCF E3 ligases. K48-specific Ube2R1 has a short about 12 amino acid insertion proximal to the E2 active site that determines specificity
-
-
-
additional information
?
-
the enzyme interacts with E3 ligases of types RING, HECT, and RBR. Ube2R2 is a K48 Ub chain-building enzyme. Ube2R1 is the cognate E2 of SCF E3 ligases. K48-specific Ube2R1 has a short about 12 amino acid insertion proximal to the E2 active site that determines specificity
-
-
-
additional information
?
-
the enzyme interacts with E3 ligases of types RING, HECT, and RBR. Ube2R2 is a K48 Ub chain-building enzyme. Ube2R1 is the cognate E2 of SCF E3 ligases. K48-specific Ube2R1 has a short about 12 amino acid insertion proximal to the E2 active site that determines specificity
-
-
-
additional information
?
-
the enzyme interacts with E3 ligases of types RING, HECT, and RBR. Ube2R2 is a K48 Ub chain-building enzyme. Ube2R1 is the cognate E2 of SCF E3 ligases. K48-specific Ube2R1 has a short about 12 amino acid insertion proximal to the E2 active site that determines specificity
-
-
-
additional information
?
-
the enzyme interacts with E3 ligases of types RING, HECT, and RBR. Ube2R2 is a K48 Ub chain-building enzyme. Ube2R1 is the cognate E2 of SCF E3 ligases. K48-specific Ube2R1 has a short about 12 amino acid insertion proximal to the E2 active site that determines specificity
-
-
-
additional information
?
-
the enzyme interacts with E3 ligases of types RING, HECT, and RBR. Ube2R2 is a K48 Ub chain-building enzyme. Ube2R1 is the cognate E2 of SCF E3 ligases. K48-specific Ube2R1 has a short about 12 amino acid insertion proximal to the E2 active site that determines specificity
-
-
-
additional information
?
-
the enzyme interacts with E3 ligases of types RING, HECT, and RBR. Ube2R2 is a K48 Ub chain-building enzyme. Ube2R1 is the cognate E2 of SCF E3 ligases. K48-specific Ube2R1 has a short about 12 amino acid insertion proximal to the E2 active site that determines specificity
-
-
-
additional information
?
-
the enzyme interacts with E3 ligases of types RING, HECT, and RBR. Ube2R2 is a K48 Ub chain-building enzyme. Ube2R1 is the cognate E2 of SCF E3 ligases. K48-specific Ube2R1 has a short about 12 amino acid insertion proximal to the E2 active site that determines specificity
-
-
-
additional information
?
-
the enzyme interacts with E3 ligases of types RING, HECT, and RBR. Ube2R2 is a K48 Ub chain-building enzyme. Ube2R1 is the cognate E2 of SCF E3 ligases. K48-specific Ube2R1 has a short about 12 amino acid insertion proximal to the E2 active site that determines specificity
-
-
-
additional information
?
-
the enzyme interacts with E3 ligases of types RING, HECT, and RBR. Ube2R2 is a K48 Ub chain-building enzyme. Ube2R1 is the cognate E2 of SCF E3 ligases. K48-specific Ube2R1 has a short about 12 amino acid insertion proximal to the E2 active site that determines specificity
-
-
-
additional information
?
-
the enzyme interacts with E3 ligases of types RING, HECT, and RBR. Ube2R2 is a K48 Ub chain-building enzyme. Ube2R1 is the cognate E2 of SCF E3 ligases. K48-specific Ube2R1 has a short about 12 amino acid insertion proximal to the E2 active site that determines specificity
-
-
-
additional information
?
-
the enzyme interacts with E3 ligases of types RING, HECT, and RBR. Ube2R2 is a K48 Ub chain-building enzyme. Ube2R1 is the cognate E2 of SCF E3 ligases. K48-specific Ube2R1 has a short about 12 amino acid insertion proximal to the E2 active site that determines specificity
-
-
-
additional information
?
-
the enzyme interacts with E3 ligases of types RING, HECT, and RBR. Ube2R2 is a K48 Ub chain-building enzyme. Ube2R1 is the cognate E2 of SCF E3 ligases. K48-specific Ube2R1 has a short about 12 amino acid insertion proximal to the E2 active site that determines specificity
-
-
-
additional information
?
-
the enzyme interacts with E3 ligases of types RING, HECT, and RBR. Ube2R2 is a K48 Ub chain-building enzyme. Ube2R1 is the cognate E2 of SCF E3 ligases. K48-specific Ube2R1 has a short about 12 amino acid insertion proximal to the E2 active site that determines specificity
-
-
-
additional information
?
-
the enzyme interacts with E3 ligases of types RING, HECT, and RBR. Ube2S is a K11 Ub chain-building enzyme. highly specific chain builders such as Ube2N, Ube2S, and Ube2R1 can only transfer their conjugated Ub to another Ub molecule
-
-
-
additional information
?
-
the enzyme interacts with E3 ligases of types RING, HECT, and RBR. Ube2S is a K11 Ub chain-building enzyme. highly specific chain builders such as Ube2N, Ube2S, and Ube2R1 can only transfer their conjugated Ub to another Ub molecule
-
-
-
additional information
?
-
the enzyme interacts with E3 ligases of types RING, HECT, and RBR. Ube2S is a K11 Ub chain-building enzyme. highly specific chain builders such as Ube2N, Ube2S, and Ube2R1 can only transfer their conjugated Ub to another Ub molecule
-
-
-
additional information
?
-
the enzyme interacts with E3 ligases of types RING, HECT, and RBR. Ube2S is a K11 Ub chain-building enzyme. highly specific chain builders such as Ube2N, Ube2S, and Ube2R1 can only transfer their conjugated Ub to another Ub molecule
-
-
-
additional information
?
-
the enzyme interacts with E3 ligases of types RING, HECT, and RBR. Ube2S is a K11 Ub chain-building enzyme. highly specific chain builders such as Ube2N, Ube2S, and Ube2R1 can only transfer their conjugated Ub to another Ub molecule
-
-
-
additional information
?
-
the enzyme interacts with E3 ligases of types RING, HECT, and RBR. Ube2S is a K11 Ub chain-building enzyme. highly specific chain builders such as Ube2N, Ube2S, and Ube2R1 can only transfer their conjugated Ub to another Ub molecule
-
-
-
additional information
?
-
the enzyme interacts with E3 ligases of types RING, HECT, and RBR. Ube2S is a K11 Ub chain-building enzyme. highly specific chain builders such as Ube2N, Ube2S, and Ube2R1 can only transfer their conjugated Ub to another Ub molecule
-
-
-
additional information
?
-
the enzyme interacts with E3 ligases of types RING, HECT, and RBR. Ube2S is a K11 Ub chain-building enzyme. highly specific chain builders such as Ube2N, Ube2S, and Ube2R1 can only transfer their conjugated Ub to another Ub molecule
-
-
-
additional information
?
-
the enzyme interacts with E3 ligases of types RING, HECT, and RBR. Ube2S is a K11 Ub chain-building enzyme. highly specific chain builders such as Ube2N, Ube2S, and Ube2R1 can only transfer their conjugated Ub to another Ub molecule
-
-
-
additional information
?
-
the enzyme interacts with E3 ligases of types RING, HECT, and RBR. Ube2S is a K11 Ub chain-building enzyme. highly specific chain builders such as Ube2N, Ube2S, and Ube2R1 can only transfer their conjugated Ub to another Ub molecule
-
-
-
additional information
?
-
the enzyme interacts with E3 ligases of types RING, HECT, and RBR. Ube2S is a K11 Ub chain-building enzyme. highly specific chain builders such as Ube2N, Ube2S, and Ube2R1 can only transfer their conjugated Ub to another Ub molecule
-
-
-
additional information
?
-
the enzyme interacts with E3 ligases of types RING, HECT, and RBR. Ube2S is a K11 Ub chain-building enzyme. highly specific chain builders such as Ube2N, Ube2S, and Ube2R1 can only transfer their conjugated Ub to another Ub molecule
-
-
-
additional information
?
-
the enzyme interacts with E3 ligases of types RING, HECT, and RBR. Ube2S is a K11 Ub chain-building enzyme. highly specific chain builders such as Ube2N, Ube2S, and Ube2R1 can only transfer their conjugated Ub to another Ub molecule
-
-
-
additional information
?
-
the enzyme interacts with E3 ligases of types RING, HECT, and RBR. Ube2S is a K11 Ub chain-building enzyme. highly specific chain builders such as Ube2N, Ube2S, and Ube2R1 can only transfer their conjugated Ub to another Ub molecule
-
-
-
additional information
?
-
the enzyme interacts with E3 ligases of types RING, HECT, and RBR. Ube2S is a K11 Ub chain-building enzyme. highly specific chain builders such as Ube2N, Ube2S, and Ube2R1 can only transfer their conjugated Ub to another Ub molecule
-
-
-
additional information
?
-
the enzyme interacts with E3 ligases of types RING, HECT, and RBR. Ube2S is a K11 Ub chain-building enzyme. highly specific chain builders such as Ube2N, Ube2S, and Ube2R1 can only transfer their conjugated Ub to another Ub molecule
-
-
-
additional information
?
-
the enzyme interacts with E3 ligases of types RING, HECT, and RBR. Ube2S is a K11 Ub chain-building enzyme. highly specific chain builders such as Ube2N, Ube2S, and Ube2R1 can only transfer their conjugated Ub to another Ub molecule
-
-
-
additional information
?
-
the enzyme interacts with E3 ligases of types RING, HECT, and RBR. Ube2S is a K11 Ub chain-building enzyme. highly specific chain builders such as Ube2N, Ube2S, and Ube2R1 can only transfer their conjugated Ub to another Ub molecule
-
-
-
additional information
?
-
the enzyme interacts with E3 ligases of types RING, HECT, and RBR. Ube2S is a K11 Ub chain-building enzyme. highly specific chain builders such as Ube2N, Ube2S, and Ube2R1 can only transfer their conjugated Ub to another Ub molecule
-
-
-
additional information
?
-
the enzyme interacts with E3 ligases of types RING, HECT, and RBR. Ube2S is a K11 Ub chain-building enzyme. highly specific chain builders such as Ube2N, Ube2S, and Ube2R1 can only transfer their conjugated Ub to another Ub molecule
-
-
-
additional information
?
-
the enzyme interacts with E3 ligases of types RING, HECT, and RBR. Ube2S is a K11 Ub chain-building enzyme. highly specific chain builders such as Ube2N, Ube2S, and Ube2R1 can only transfer their conjugated Ub to another Ub molecule
-
-
-
additional information
?
-
the enzyme interacts with E3 ligases of types RING, HECT, and RBR. Ube2S is a K11 Ub chain-building enzyme. highly specific chain builders such as Ube2N, Ube2S, and Ube2R1 can only transfer their conjugated Ub to another Ub molecule
-
-
-
additional information
?
-
the enzyme interacts with E3 ligases of types RING, HECT, and RBR. Ube2S is a K11 Ub chain-building enzyme. highly specific chain builders such as Ube2N, Ube2S, and Ube2R1 can only transfer their conjugated Ub to another Ub molecule
-
-
-
additional information
?
-
the enzyme interacts with E3 ligases of types RING, HECT, and RBR. Ube2S is a K11 Ub chain-building enzyme. highly specific chain builders such as Ube2N, Ube2S, and Ube2R1 can only transfer their conjugated Ub to another Ub molecule
-
-
-
additional information
?
-
the enzyme interacts with E3 ligases of types RING, HECT, and RBR. Ube2S is a K11 Ub chain-building enzyme. highly specific chain builders such as Ube2N, Ube2S, and Ube2R1 can only transfer their conjugated Ub to another Ub molecule
-
-
-
additional information
?
-
the enzyme interacts with E3 ligases of types RING, HECT, and RBR. Ube2S is a K11 Ub chain-building enzyme. highly specific chain builders such as Ube2N, Ube2S, and Ube2R1 can only transfer their conjugated Ub to another Ub molecule
-
-
-
additional information
?
-
the enzyme interacts with E3 ligases of types RING, HECT, and RBR. Ube2S is a K11 Ub chain-building enzyme. highly specific chain builders such as Ube2N, Ube2S, and Ube2R1 can only transfer their conjugated Ub to another Ub molecule
-
-
-
additional information
?
-
the enzyme interacts with E3 ligases of types RING, HECT, and RBR. Ube2S is a K11 Ub chain-building enzyme. highly specific chain builders such as Ube2N, Ube2S, and Ube2R1 can only transfer their conjugated Ub to another Ub molecule
-
-
-
additional information
?
-
the enzyme interacts with E3 ligases of types RING, HECT, and RBR. Ube2S is a K11 Ub chain-building enzyme. highly specific chain builders such as Ube2N, Ube2S, and Ube2R1 can only transfer their conjugated Ub to another Ub molecule
-
-
-
additional information
?
-
the enzyme interacts with E3 ligases of types RING, HECT, and RBR. Ube2S is a K11 Ub chain-building enzyme. highly specific chain builders such as Ube2N, Ube2S, and Ube2R1 can only transfer their conjugated Ub to another Ub molecule
-
-
-
additional information
?
-
the enzyme interacts with E3 ligases of types RING, HECT, and RBR. Ube2T monoubiquitylates its substrate FANCD2 on a specific lysine with its RING E3 FANCL in the Fanconi Anemia DNA repair pathway
-
-
-
additional information
?
-
the enzyme interacts with E3 ligases of types RING, HECT, and RBR. Ube2T monoubiquitylates its substrate FANCD2 on a specific lysine with its RING E3 FANCL in the Fanconi Anemia DNA repair pathway
-
-
-
additional information
?
-
the enzyme interacts with E3 ligases of types RING, HECT, and RBR. Ube2T monoubiquitylates its substrate FANCD2 on a specific lysine with its RING E3 FANCL in the Fanconi Anemia DNA repair pathway
-
-
-
additional information
?
-
the enzyme interacts with E3 ligases of types RING, HECT, and RBR. Ube2T monoubiquitylates its substrate FANCD2 on a specific lysine with its RING E3 FANCL in the Fanconi Anemia DNA repair pathway
-
-
-
additional information
?
-
the enzyme interacts with E3 ligases of types RING, HECT, and RBR. Ube2T monoubiquitylates its substrate FANCD2 on a specific lysine with its RING E3 FANCL in the Fanconi Anemia DNA repair pathway
-
-
-
additional information
?
-
the enzyme interacts with E3 ligases of types RING, HECT, and RBR. Ube2T monoubiquitylates its substrate FANCD2 on a specific lysine with its RING E3 FANCL in the Fanconi Anemia DNA repair pathway
-
-
-
additional information
?
-
the enzyme interacts with E3 ligases of types RING, HECT, and RBR. Ube2T monoubiquitylates its substrate FANCD2 on a specific lysine with its RING E3 FANCL in the Fanconi Anemia DNA repair pathway
-
-
-
additional information
?
-
the enzyme interacts with E3 ligases of types RING, HECT, and RBR. Ube2T monoubiquitylates its substrate FANCD2 on a specific lysine with its RING E3 FANCL in the Fanconi Anemia DNA repair pathway
-
-
-
additional information
?
-
the enzyme interacts with E3 ligases of types RING, HECT, and RBR. Ube2T monoubiquitylates its substrate FANCD2 on a specific lysine with its RING E3 FANCL in the Fanconi Anemia DNA repair pathway
-
-
-
additional information
?
-
the enzyme interacts with E3 ligases of types RING, HECT, and RBR. Ube2T monoubiquitylates its substrate FANCD2 on a specific lysine with its RING E3 FANCL in the Fanconi Anemia DNA repair pathway
-
-
-
additional information
?
-
the enzyme interacts with E3 ligases of types RING, HECT, and RBR. Ube2T monoubiquitylates its substrate FANCD2 on a specific lysine with its RING E3 FANCL in the Fanconi Anemia DNA repair pathway
-
-
-
additional information
?
-
the enzyme interacts with E3 ligases of types RING, HECT, and RBR. Ube2T monoubiquitylates its substrate FANCD2 on a specific lysine with its RING E3 FANCL in the Fanconi Anemia DNA repair pathway
-
-
-
additional information
?
-
the enzyme interacts with E3 ligases of types RING, HECT, and RBR. Ube2T monoubiquitylates its substrate FANCD2 on a specific lysine with its RING E3 FANCL in the Fanconi Anemia DNA repair pathway
-
-
-
additional information
?
-
the enzyme interacts with E3 ligases of types RING, HECT, and RBR. Ube2T monoubiquitylates its substrate FANCD2 on a specific lysine with its RING E3 FANCL in the Fanconi Anemia DNA repair pathway
-
-
-
additional information
?
-
the enzyme interacts with E3 ligases of types RING, HECT, and RBR. Ube2T monoubiquitylates its substrate FANCD2 on a specific lysine with its RING E3 FANCL in the Fanconi Anemia DNA repair pathway
-
-
-
additional information
?
-
the enzyme interacts with E3 ligases of types RING, HECT, and RBR. Ube2T monoubiquitylates its substrate FANCD2 on a specific lysine with its RING E3 FANCL in the Fanconi Anemia DNA repair pathway
-
-
-
additional information
?
-
the enzyme interacts with E3 ligases of types RING, HECT, and RBR. Ube2T monoubiquitylates its substrate FANCD2 on a specific lysine with its RING E3 FANCL in the Fanconi Anemia DNA repair pathway
-
-
-
additional information
?
-
the enzyme interacts with E3 ligases of types RING, HECT, and RBR. Ube2T monoubiquitylates its substrate FANCD2 on a specific lysine with its RING E3 FANCL in the Fanconi Anemia DNA repair pathway
-
-
-
additional information
?
-
the enzyme interacts with E3 ligases of types RING, HECT, and RBR. Ube2T monoubiquitylates its substrate FANCD2 on a specific lysine with its RING E3 FANCL in the Fanconi Anemia DNA repair pathway
-
-
-
additional information
?
-
the enzyme interacts with E3 ligases of types RING, HECT, and RBR. Ube2T monoubiquitylates its substrate FANCD2 on a specific lysine with its RING E3 FANCL in the Fanconi Anemia DNA repair pathway
-
-
-
additional information
?
-
the enzyme interacts with E3 ligases of types RING, HECT, and RBR. Ube2T monoubiquitylates its substrate FANCD2 on a specific lysine with its RING E3 FANCL in the Fanconi Anemia DNA repair pathway
-
-
-
additional information
?
-
the enzyme interacts with E3 ligases of types RING, HECT, and RBR. Ube2T monoubiquitylates its substrate FANCD2 on a specific lysine with its RING E3 FANCL in the Fanconi Anemia DNA repair pathway
-
-
-
additional information
?
-
the enzyme interacts with E3 ligases of types RING, HECT, and RBR. Ube2T monoubiquitylates its substrate FANCD2 on a specific lysine with its RING E3 FANCL in the Fanconi Anemia DNA repair pathway
-
-
-
additional information
?
-
the enzyme interacts with E3 ligases of types RING, HECT, and RBR. Ube2T monoubiquitylates its substrate FANCD2 on a specific lysine with its RING E3 FANCL in the Fanconi Anemia DNA repair pathway
-
-
-
additional information
?
-
the enzyme interacts with E3 ligases of types RING, HECT, and RBR. Ube2T monoubiquitylates its substrate FANCD2 on a specific lysine with its RING E3 FANCL in the Fanconi Anemia DNA repair pathway
-
-
-
additional information
?
-
the enzyme interacts with E3 ligases of types RING, HECT, and RBR. Ube2T monoubiquitylates its substrate FANCD2 on a specific lysine with its RING E3 FANCL in the Fanconi Anemia DNA repair pathway
-
-
-
additional information
?
-
the enzyme interacts with E3 ligases of types RING, HECT, and RBR. Ube2T monoubiquitylates its substrate FANCD2 on a specific lysine with its RING E3 FANCL in the Fanconi Anemia DNA repair pathway
-
-
-
additional information
?
-
the enzyme interacts with E3 ligases of types RING, HECT, and RBR. Ube2T monoubiquitylates its substrate FANCD2 on a specific lysine with its RING E3 FANCL in the Fanconi Anemia DNA repair pathway
-
-
-
additional information
?
-
the enzyme interacts with E3 ligases of types RING, HECT, and RBR. Ube2T monoubiquitylates its substrate FANCD2 on a specific lysine with its RING E3 FANCL in the Fanconi Anemia DNA repair pathway
-
-
-
additional information
?
-
the enzyme interacts with E3 ligases of types RING, HECT, and RBR. Ube2T monoubiquitylates its substrate FANCD2 on a specific lysine with its RING E3 FANCL in the Fanconi Anemia DNA repair pathway
-
-
-
additional information
?
-
the enzyme interacts with the C-terminal extension. Ube2Z is a bispecific E2 active with FAT10 (ubiquitin D) and ubiquitin (Ub)
-
-
-
additional information
?
-
the enzyme interacts with the C-terminal extension. Ube2Z is a bispecific E2 active with FAT10 (ubiquitin D) and ubiquitin (Ub)
-
-
-
additional information
?
-
the enzyme interacts with the C-terminal extension. Ube2Z is a bispecific E2 active with FAT10 (ubiquitin D) and ubiquitin (Ub)
-
-
-
additional information
?
-
the enzyme interacts with the C-terminal extension. Ube2Z is a bispecific E2 active with FAT10 (ubiquitin D) and ubiquitin (Ub)
-
-
-
additional information
?
-
the enzyme interacts with the C-terminal extension. Ube2Z is a bispecific E2 active with FAT10 (ubiquitin D) and ubiquitin (Ub)
-
-
-
additional information
?
-
the enzyme interacts with the C-terminal extension. Ube2Z is a bispecific E2 active with FAT10 (ubiquitin D) and ubiquitin (Ub)
-
-
-
additional information
?
-
the enzyme interacts with the C-terminal extension. Ube2Z is a bispecific E2 active with FAT10 (ubiquitin D) and ubiquitin (Ub)
-
-
-
additional information
?
-
the enzyme interacts with the C-terminal extension. Ube2Z is a bispecific E2 active with FAT10 (ubiquitin D) and ubiquitin (Ub)
-
-
-
additional information
?
-
the enzyme interacts with the C-terminal extension. Ube2Z is a bispecific E2 active with FAT10 (ubiquitin D) and ubiquitin (Ub)
-
-
-
additional information
?
-
the enzyme interacts with the C-terminal extension. Ube2Z is a bispecific E2 active with FAT10 (ubiquitin D) and ubiquitin (Ub)
-
-
-
additional information
?
-
the enzyme interacts with the C-terminal extension. Ube2Z is a bispecific E2 active with FAT10 (ubiquitin D) and ubiquitin (Ub)
-
-
-
additional information
?
-
the enzyme interacts with the C-terminal extension. Ube2Z is a bispecific E2 active with FAT10 (ubiquitin D) and ubiquitin (Ub)
-
-
-
additional information
?
-
the enzyme interacts with the C-terminal extension. Ube2Z is a bispecific E2 active with FAT10 (ubiquitin D) and ubiquitin (Ub)
-
-
-
additional information
?
-
the enzyme interacts with the C-terminal extension. Ube2Z is a bispecific E2 active with FAT10 (ubiquitin D) and ubiquitin (Ub)
-
-
-
additional information
?
-
the enzyme interacts with the C-terminal extension. Ube2Z is a bispecific E2 active with FAT10 (ubiquitin D) and ubiquitin (Ub)
-
-
-
additional information
?
-
the enzyme interacts with the C-terminal extension. Ube2Z is a bispecific E2 active with FAT10 (ubiquitin D) and ubiquitin (Ub)
-
-
-
additional information
?
-
the enzyme interacts with the C-terminal extension. Ube2Z is a bispecific E2 active with FAT10 (ubiquitin D) and ubiquitin (Ub)
-
-
-
additional information
?
-
the enzyme interacts with the C-terminal extension. Ube2Z is a bispecific E2 active with FAT10 (ubiquitin D) and ubiquitin (Ub)
-
-
-
additional information
?
-
the enzyme interacts with the C-terminal extension. Ube2Z is a bispecific E2 active with FAT10 (ubiquitin D) and ubiquitin (Ub)
-
-
-
additional information
?
-
the enzyme interacts with the C-terminal extension. Ube2Z is a bispecific E2 active with FAT10 (ubiquitin D) and ubiquitin (Ub)
-
-
-
additional information
?
-
the enzyme interacts with the C-terminal extension. Ube2Z is a bispecific E2 active with FAT10 (ubiquitin D) and ubiquitin (Ub)
-
-
-
additional information
?
-
the enzyme interacts with the C-terminal extension. Ube2Z is a bispecific E2 active with FAT10 (ubiquitin D) and ubiquitin (Ub)
-
-
-
additional information
?
-
the enzyme interacts with the C-terminal extension. Ube2Z is a bispecific E2 active with FAT10 (ubiquitin D) and ubiquitin (Ub)
-
-
-
additional information
?
-
the enzyme interacts with the C-terminal extension. Ube2Z is a bispecific E2 active with FAT10 (ubiquitin D) and ubiquitin (Ub)
-
-
-
additional information
?
-
the enzyme interacts with the C-terminal extension. Ube2Z is a bispecific E2 active with FAT10 (ubiquitin D) and ubiquitin (Ub)
-
-
-
additional information
?
-
the enzyme interacts with the C-terminal extension. Ube2Z is a bispecific E2 active with FAT10 (ubiquitin D) and ubiquitin (Ub)
-
-
-
additional information
?
-
the enzyme interacts with the C-terminal extension. Ube2Z is a bispecific E2 active with FAT10 (ubiquitin D) and ubiquitin (Ub)
-
-
-
additional information
?
-
the enzyme interacts with the C-terminal extension. Ube2Z is a bispecific E2 active with FAT10 (ubiquitin D) and ubiquitin (Ub)
-
-
-
additional information
?
-
the enzyme interacts with the C-terminal extension. Ube2Z is a bispecific E2 active with FAT10 (ubiquitin D) and ubiquitin (Ub)
-
-
-
additional information
?
-
the enzyme interacts with the C-terminal extension. Ube2Z is a bispecific E2 active with FAT10 (ubiquitin D) and ubiquitin (Ub)
-
-
-
additional information
?
-
the enzyme interacts with ubiquitin and E3 ligases, of types RING, HECT, RBR. The preference of Ube2E3 to generate monoubiquitylated products arises from specific interactions involving K48 on Ub and backside residues of the E2
-
-
-
additional information
?
-
the enzyme interacts with ubiquitin and E3 ligases, of types RING, HECT, RBR. The preference of Ube2E3 to generate monoubiquitylated products arises from specific interactions involving K48 on Ub and backside residues of the E2
-
-
-
additional information
?
-
the enzyme interacts with ubiquitin and E3 ligases, of types RING, HECT, RBR. The preference of Ube2E3 to generate monoubiquitylated products arises from specific interactions involving K48 on Ub and backside residues of the E2
-
-
-
additional information
?
-
the enzyme interacts with ubiquitin and E3 ligases, of types RING, HECT, RBR. The preference of Ube2E3 to generate monoubiquitylated products arises from specific interactions involving K48 on Ub and backside residues of the E2
-
-
-
additional information
?
-
the enzyme interacts with ubiquitin and E3 ligases, of types RING, HECT, RBR. The preference of Ube2E3 to generate monoubiquitylated products arises from specific interactions involving K48 on Ub and backside residues of the E2
-
-
-
additional information
?
-
the enzyme interacts with ubiquitin and E3 ligases, of types RING, HECT, RBR. The preference of Ube2E3 to generate monoubiquitylated products arises from specific interactions involving K48 on Ub and backside residues of the E2
-
-
-
additional information
?
-
the enzyme interacts with ubiquitin and E3 ligases, of types RING, HECT, RBR. The preference of Ube2E3 to generate monoubiquitylated products arises from specific interactions involving K48 on Ub and backside residues of the E2
-
-
-
additional information
?
-
the enzyme interacts with ubiquitin and E3 ligases, of types RING, HECT, RBR. The preference of Ube2E3 to generate monoubiquitylated products arises from specific interactions involving K48 on Ub and backside residues of the E2
-
-
-
additional information
?
-
the enzyme interacts with ubiquitin and E3 ligases, of types RING, HECT, RBR. The preference of Ube2E3 to generate monoubiquitylated products arises from specific interactions involving K48 on Ub and backside residues of the E2
-
-
-
additional information
?
-
the enzyme interacts with ubiquitin and E3 ligases, of types RING, HECT, RBR. The preference of Ube2E3 to generate monoubiquitylated products arises from specific interactions involving K48 on Ub and backside residues of the E2
-
-
-
additional information
?
-
the enzyme interacts with ubiquitin and E3 ligases, of types RING, HECT, RBR. The preference of Ube2E3 to generate monoubiquitylated products arises from specific interactions involving K48 on Ub and backside residues of the E2
-
-
-
additional information
?
-
the enzyme interacts with ubiquitin and E3 ligases, of types RING, HECT, RBR. The preference of Ube2E3 to generate monoubiquitylated products arises from specific interactions involving K48 on Ub and backside residues of the E2
-
-
-
additional information
?
-
the enzyme interacts with ubiquitin and E3 ligases, of types RING, HECT, RBR. The preference of Ube2E3 to generate monoubiquitylated products arises from specific interactions involving K48 on Ub and backside residues of the E2
-
-
-
additional information
?
-
the enzyme interacts with ubiquitin and E3 ligases, of types RING, HECT, RBR. The preference of Ube2E3 to generate monoubiquitylated products arises from specific interactions involving K48 on Ub and backside residues of the E2
-
-
-
additional information
?
-
the enzyme interacts with ubiquitin and E3 ligases, of types RING, HECT, RBR. The preference of Ube2E3 to generate monoubiquitylated products arises from specific interactions involving K48 on Ub and backside residues of the E2
-
-
-
additional information
?
-
the enzyme interacts with ubiquitin and E3 ligases, of types RING, HECT, RBR. The preference of Ube2E3 to generate monoubiquitylated products arises from specific interactions involving K48 on Ub and backside residues of the E2
-
-
-
additional information
?
-
the enzyme interacts with ubiquitin and E3 ligases, of types RING, HECT, RBR. The preference of Ube2E3 to generate monoubiquitylated products arises from specific interactions involving K48 on Ub and backside residues of the E2
-
-
-
additional information
?
-
the enzyme interacts with ubiquitin and E3 ligases, of types RING, HECT, RBR. The preference of Ube2E3 to generate monoubiquitylated products arises from specific interactions involving K48 on Ub and backside residues of the E2
-
-
-
additional information
?
-
the enzyme interacts with ubiquitin and E3 ligases, of types RING, HECT, RBR. The preference of Ube2E3 to generate monoubiquitylated products arises from specific interactions involving K48 on Ub and backside residues of the E2
-
-
-
additional information
?
-
the enzyme interacts with ubiquitin and E3 ligases, of types RING, HECT, RBR. The preference of Ube2E3 to generate monoubiquitylated products arises from specific interactions involving K48 on Ub and backside residues of the E2
-
-
-
additional information
?
-
the enzyme interacts with ubiquitin and E3 ligases, of types RING, HECT, RBR. The preference of Ube2E3 to generate monoubiquitylated products arises from specific interactions involving K48 on Ub and backside residues of the E2
-
-
-
additional information
?
-
the enzyme interacts with ubiquitin and E3 ligases, of types RING, HECT, RBR. The preference of Ube2E3 to generate monoubiquitylated products arises from specific interactions involving K48 on Ub and backside residues of the E2
-
-
-
additional information
?
-
the enzyme interacts with ubiquitin and E3 ligases, of types RING, HECT, RBR. The preference of Ube2E3 to generate monoubiquitylated products arises from specific interactions involving K48 on Ub and backside residues of the E2
-
-
-
additional information
?
-
the enzyme interacts with ubiquitin and E3 ligases, of types RING, HECT, RBR. The preference of Ube2E3 to generate monoubiquitylated products arises from specific interactions involving K48 on Ub and backside residues of the E2
-
-
-
additional information
?
-
the enzyme interacts with ubiquitin and E3 ligases, of types RING, HECT, RBR. The preference of Ube2E3 to generate monoubiquitylated products arises from specific interactions involving K48 on Ub and backside residues of the E2
-
-
-
additional information
?
-
the enzyme interacts with ubiquitin and E3 ligases, of types RING, HECT, RBR. The preference of Ube2E3 to generate monoubiquitylated products arises from specific interactions involving K48 on Ub and backside residues of the E2
-
-
-
additional information
?
-
the enzyme interacts with ubiquitin and E3 ligases, of types RING, HECT, RBR. The preference of Ube2E3 to generate monoubiquitylated products arises from specific interactions involving K48 on Ub and backside residues of the E2
-
-
-
additional information
?
-
the enzyme interacts with ubiquitin and E3 ligases, of types RING, HECT, RBR. The preference of Ube2E3 to generate monoubiquitylated products arises from specific interactions involving K48 on Ub and backside residues of the E2
-
-
-
additional information
?
-
the enzyme interacts with ubiquitin and E3 ligases, of types RING, HECT, RBR. The preference of Ube2E3 to generate monoubiquitylated products arises from specific interactions involving K48 on Ub and backside residues of the E2
-
-
-
additional information
?
-
the enzyme interacts with ubiquitin and E3 ligases, of types RING, HECT, RBR. The preference of Ube2E3 to generate monoubiquitylated products arises from specific interactions involving K48 on Ub and backside residues of the E2
-
-
-
additional information
?
-
the enzyme interacts with ubiquitin, and E3 ligases of types RING, HECT, and RBR
-
-
-
additional information
?
-
the enzyme interacts with ubiquitin, and E3 ligases of types RING, HECT, and RBR
-
-
-
additional information
?
-
the enzyme interacts with ubiquitin, and E3 ligases of types RING, HECT, and RBR
-
-
-
additional information
?
-
the enzyme interacts with ubiquitin, and E3 ligases of types RING, HECT, and RBR
-
-
-
additional information
?
-
the enzyme interacts with ubiquitin, and E3 ligases of types RING, HECT, and RBR
-
-
-
additional information
?
-
the enzyme interacts with ubiquitin, and E3 ligases of types RING, HECT, and RBR
-
-
-
additional information
?
-
the enzyme interacts with ubiquitin, and E3 ligases of types RING, HECT, and RBR
-
-
-
additional information
?
-
the enzyme interacts with ubiquitin, and E3 ligases of types RING, HECT, and RBR
-
-
-
additional information
?
-
the enzyme interacts with ubiquitin, and E3 ligases of types RING, HECT, and RBR
-
-
-
additional information
?
-
the enzyme interacts with ubiquitin, and E3 ligases of types RING, HECT, and RBR
-
-
-
additional information
?
-
the enzyme interacts with ubiquitin, and E3 ligases of types RING, HECT, and RBR
-
-
-
additional information
?
-
the enzyme interacts with ubiquitin, and E3 ligases of types RING, HECT, and RBR
-
-
-
additional information
?
-
the enzyme interacts with ubiquitin, and E3 ligases of types RING, HECT, and RBR
-
-
-
additional information
?
-
the enzyme interacts with ubiquitin, and E3 ligases of types RING, HECT, and RBR
-
-
-
additional information
?
-
the enzyme interacts with ubiquitin, and E3 ligases of types RING, HECT, and RBR
-
-
-
additional information
?
-
the enzyme interacts with ubiquitin, and E3 ligases of types RING, HECT, and RBR
-
-
-
additional information
?
-
the enzyme interacts with ubiquitin, and E3 ligases of types RING, HECT, and RBR
-
-
-
additional information
?
-
the enzyme interacts with ubiquitin, and E3 ligases of types RING, HECT, and RBR
-
-
-
additional information
?
-
the enzyme interacts with ubiquitin, and E3 ligases of types RING, HECT, and RBR
-
-
-
additional information
?
-
the enzyme interacts with ubiquitin, and E3 ligases of types RING, HECT, and RBR
-
-
-
additional information
?
-
the enzyme interacts with ubiquitin, and E3 ligases of types RING, HECT, and RBR
-
-
-
additional information
?
-
the enzyme interacts with ubiquitin, and E3 ligases of types RING, HECT, and RBR
-
-
-
additional information
?
-
the enzyme interacts with ubiquitin, and E3 ligases of types RING, HECT, and RBR
-
-
-
additional information
?
-
the enzyme interacts with ubiquitin, and E3 ligases of types RING, HECT, and RBR
-
-
-
additional information
?
-
the enzyme interacts with ubiquitin, and E3 ligases of types RING, HECT, and RBR
-
-
-
additional information
?
-
the enzyme interacts with ubiquitin, and E3 ligases of types RING, HECT, and RBR
-
-
-
additional information
?
-
the enzyme interacts with ubiquitin, and E3 ligases of types RING, HECT, and RBR
-
-
-
additional information
?
-
the enzyme interacts with ubiquitin, and E3 ligases of types RING, HECT, and RBR
-
-
-
additional information
?
-
the enzyme interacts with ubiquitin, and E3 ligases of types RING, HECT, and RBR
-
-
-
additional information
?
-
the enzyme interacts with ubiquitin, and E3 ligases of types RING, HECT, and RBR
-
-
-
additional information
?
-
the enzyme interacts with ubiquitin, and E3 ligases of types RING, HECT, and RBR. Backside binding by Ub increases the intrinsic lysine reactivity of Ube2D2-Ub, indicating an allosteric effect
-
-
-
additional information
?
-
the enzyme interacts with ubiquitin, and E3 ligases of types RING, HECT, and RBR. Backside binding by Ub increases the intrinsic lysine reactivity of Ube2D2-Ub, indicating an allosteric effect
-
-
-
additional information
?
-
the enzyme interacts with ubiquitin, and E3 ligases of types RING, HECT, and RBR. Backside binding by Ub increases the intrinsic lysine reactivity of Ube2D2-Ub, indicating an allosteric effect
-
-
-
additional information
?
-
the enzyme interacts with ubiquitin, and E3 ligases of types RING, HECT, and RBR. Backside binding by Ub increases the intrinsic lysine reactivity of Ube2D2-Ub, indicating an allosteric effect
-
-
-
additional information
?
-
the enzyme interacts with ubiquitin, and E3 ligases of types RING, HECT, and RBR. Backside binding by Ub increases the intrinsic lysine reactivity of Ube2D2-Ub, indicating an allosteric effect
-
-
-
additional information
?
-
the enzyme interacts with ubiquitin, and E3 ligases of types RING, HECT, and RBR. Backside binding by Ub increases the intrinsic lysine reactivity of Ube2D2-Ub, indicating an allosteric effect
-
-
-
additional information
?
-
the enzyme interacts with ubiquitin, and E3 ligases of types RING, HECT, and RBR. Backside binding by Ub increases the intrinsic lysine reactivity of Ube2D2-Ub, indicating an allosteric effect
-
-
-
additional information
?
-
the enzyme interacts with ubiquitin, and E3 ligases of types RING, HECT, and RBR. Backside binding by Ub increases the intrinsic lysine reactivity of Ube2D2-Ub, indicating an allosteric effect
-
-
-
additional information
?
-
the enzyme interacts with ubiquitin, and E3 ligases of types RING, HECT, and RBR. Backside binding by Ub increases the intrinsic lysine reactivity of Ube2D2-Ub, indicating an allosteric effect
-
-
-
additional information
?
-
the enzyme interacts with ubiquitin, and E3 ligases of types RING, HECT, and RBR. Backside binding by Ub increases the intrinsic lysine reactivity of Ube2D2-Ub, indicating an allosteric effect
-
-
-
additional information
?
-
the enzyme interacts with ubiquitin, and E3 ligases of types RING, HECT, and RBR. Backside binding by Ub increases the intrinsic lysine reactivity of Ube2D2-Ub, indicating an allosteric effect
-
-
-
additional information
?
-
the enzyme interacts with ubiquitin, and E3 ligases of types RING, HECT, and RBR. Backside binding by Ub increases the intrinsic lysine reactivity of Ube2D2-Ub, indicating an allosteric effect
-
-
-
additional information
?
-
the enzyme interacts with ubiquitin, and E3 ligases of types RING, HECT, and RBR. Backside binding by Ub increases the intrinsic lysine reactivity of Ube2D2-Ub, indicating an allosteric effect
-
-
-
additional information
?
-
the enzyme interacts with ubiquitin, and E3 ligases of types RING, HECT, and RBR. Backside binding by Ub increases the intrinsic lysine reactivity of Ube2D2-Ub, indicating an allosteric effect
-
-
-
additional information
?
-
the enzyme interacts with ubiquitin, and E3 ligases of types RING, HECT, and RBR. Backside binding by Ub increases the intrinsic lysine reactivity of Ube2D2-Ub, indicating an allosteric effect
-
-
-
additional information
?
-
the enzyme interacts with ubiquitin, and E3 ligases of types RING, HECT, and RBR. Backside binding by Ub increases the intrinsic lysine reactivity of Ube2D2-Ub, indicating an allosteric effect
-
-
-
additional information
?
-
the enzyme interacts with ubiquitin, and E3 ligases of types RING, HECT, and RBR. Backside binding by Ub increases the intrinsic lysine reactivity of Ube2D2-Ub, indicating an allosteric effect
-
-
-
additional information
?
-
the enzyme interacts with ubiquitin, and E3 ligases of types RING, HECT, and RBR. Backside binding by Ub increases the intrinsic lysine reactivity of Ube2D2-Ub, indicating an allosteric effect
-
-
-
additional information
?
-
the enzyme interacts with ubiquitin, and E3 ligases of types RING, HECT, and RBR. Backside binding by Ub increases the intrinsic lysine reactivity of Ube2D2-Ub, indicating an allosteric effect
-
-
-
additional information
?
-
the enzyme interacts with ubiquitin, and E3 ligases of types RING, HECT, and RBR. Backside binding by Ub increases the intrinsic lysine reactivity of Ube2D2-Ub, indicating an allosteric effect
-
-
-
additional information
?
-
the enzyme interacts with ubiquitin, and E3 ligases of types RING, HECT, and RBR. Backside binding by Ub increases the intrinsic lysine reactivity of Ube2D2-Ub, indicating an allosteric effect
-
-
-
additional information
?
-
the enzyme interacts with ubiquitin, and E3 ligases of types RING, HECT, and RBR. Backside binding by Ub increases the intrinsic lysine reactivity of Ube2D2-Ub, indicating an allosteric effect
-
-
-
additional information
?
-
the enzyme interacts with ubiquitin, and E3 ligases of types RING, HECT, and RBR. Backside binding by Ub increases the intrinsic lysine reactivity of Ube2D2-Ub, indicating an allosteric effect
-
-
-
additional information
?
-
the enzyme interacts with ubiquitin, and E3 ligases of types RING, HECT, and RBR. Backside binding by Ub increases the intrinsic lysine reactivity of Ube2D2-Ub, indicating an allosteric effect
-
-
-
additional information
?
-
the enzyme interacts with ubiquitin, and E3 ligases of types RING, HECT, and RBR. Backside binding by Ub increases the intrinsic lysine reactivity of Ube2D2-Ub, indicating an allosteric effect
-
-
-
additional information
?
-
the enzyme interacts with ubiquitin, and E3 ligases of types RING, HECT, and RBR. Backside binding by Ub increases the intrinsic lysine reactivity of Ube2D2-Ub, indicating an allosteric effect
-
-
-
additional information
?
-
the enzyme interacts with ubiquitin, and E3 ligases of types RING, HECT, and RBR. Backside binding by Ub increases the intrinsic lysine reactivity of Ube2D2-Ub, indicating an allosteric effect
-
-
-
additional information
?
-
the enzyme interacts with ubiquitin, and E3 ligases of types RING, HECT, and RBR. Backside binding by Ub increases the intrinsic lysine reactivity of Ube2D2-Ub, indicating an allosteric effect
-
-
-
additional information
?
-
the enzyme interacts with ubiquitin, and E3 ligases of types RING, HECT, and RBR. Backside binding by Ub increases the intrinsic lysine reactivity of Ube2D2-Ub, indicating an allosteric effect
-
-
-
additional information
?
-
the enzyme interacts with ubiquitin, and E3 ligases of types RING, HECT, and RBR. Backside binding by Ub increases the intrinsic lysine reactivity of Ube2D2-Ub, indicating an allosteric effect
-
-
-
additional information
?
-
the enzyme interacts with ubiquitin, and E3 ligases of types RING, HECT, and RBR. Neither HECTs nor RBRs enhance the intrinsic lysine reactivity of Ube2D3. In the open conformation, Ube2D3-Ub is highly reactive towards free cysteine, but shows greatly reduced reactivity towards free lysine when compared with free Ube2D3-Ub
-
-
-
additional information
?
-
the enzyme interacts with ubiquitin, and E3 ligases of types RING, HECT, and RBR. Neither HECTs nor RBRs enhance the intrinsic lysine reactivity of Ube2D3. In the open conformation, Ube2D3-Ub is highly reactive towards free cysteine, but shows greatly reduced reactivity towards free lysine when compared with free Ube2D3-Ub
-
-
-
additional information
?
-
the enzyme interacts with ubiquitin, and E3 ligases of types RING, HECT, and RBR. Neither HECTs nor RBRs enhance the intrinsic lysine reactivity of Ube2D3. In the open conformation, Ube2D3-Ub is highly reactive towards free cysteine, but shows greatly reduced reactivity towards free lysine when compared with free Ube2D3-Ub
-
-
-
additional information
?
-
the enzyme interacts with ubiquitin, and E3 ligases of types RING, HECT, and RBR. Neither HECTs nor RBRs enhance the intrinsic lysine reactivity of Ube2D3. In the open conformation, Ube2D3-Ub is highly reactive towards free cysteine, but shows greatly reduced reactivity towards free lysine when compared with free Ube2D3-Ub
-
-
-
additional information
?
-
the enzyme interacts with ubiquitin, and E3 ligases of types RING, HECT, and RBR. Neither HECTs nor RBRs enhance the intrinsic lysine reactivity of Ube2D3. In the open conformation, Ube2D3-Ub is highly reactive towards free cysteine, but shows greatly reduced reactivity towards free lysine when compared with free Ube2D3-Ub
-
-
-
additional information
?
-
the enzyme interacts with ubiquitin, and E3 ligases of types RING, HECT, and RBR. Neither HECTs nor RBRs enhance the intrinsic lysine reactivity of Ube2D3. In the open conformation, Ube2D3-Ub is highly reactive towards free cysteine, but shows greatly reduced reactivity towards free lysine when compared with free Ube2D3-Ub
-
-
-
additional information
?
-
the enzyme interacts with ubiquitin, and E3 ligases of types RING, HECT, and RBR. Neither HECTs nor RBRs enhance the intrinsic lysine reactivity of Ube2D3. In the open conformation, Ube2D3-Ub is highly reactive towards free cysteine, but shows greatly reduced reactivity towards free lysine when compared with free Ube2D3-Ub
-
-
-
additional information
?
-
the enzyme interacts with ubiquitin, and E3 ligases of types RING, HECT, and RBR. Neither HECTs nor RBRs enhance the intrinsic lysine reactivity of Ube2D3. In the open conformation, Ube2D3-Ub is highly reactive towards free cysteine, but shows greatly reduced reactivity towards free lysine when compared with free Ube2D3-Ub
-
-
-
additional information
?
-
the enzyme interacts with ubiquitin, and E3 ligases of types RING, HECT, and RBR. Neither HECTs nor RBRs enhance the intrinsic lysine reactivity of Ube2D3. In the open conformation, Ube2D3-Ub is highly reactive towards free cysteine, but shows greatly reduced reactivity towards free lysine when compared with free Ube2D3-Ub
-
-
-
additional information
?
-
the enzyme interacts with ubiquitin, and E3 ligases of types RING, HECT, and RBR. Neither HECTs nor RBRs enhance the intrinsic lysine reactivity of Ube2D3. In the open conformation, Ube2D3-Ub is highly reactive towards free cysteine, but shows greatly reduced reactivity towards free lysine when compared with free Ube2D3-Ub
-
-
-
additional information
?
-
the enzyme interacts with ubiquitin, and E3 ligases of types RING, HECT, and RBR. Neither HECTs nor RBRs enhance the intrinsic lysine reactivity of Ube2D3. In the open conformation, Ube2D3-Ub is highly reactive towards free cysteine, but shows greatly reduced reactivity towards free lysine when compared with free Ube2D3-Ub
-
-
-
additional information
?
-
the enzyme interacts with ubiquitin, and E3 ligases of types RING, HECT, and RBR. Neither HECTs nor RBRs enhance the intrinsic lysine reactivity of Ube2D3. In the open conformation, Ube2D3-Ub is highly reactive towards free cysteine, but shows greatly reduced reactivity towards free lysine when compared with free Ube2D3-Ub
-
-
-
additional information
?
-
the enzyme interacts with ubiquitin, and E3 ligases of types RING, HECT, and RBR. Neither HECTs nor RBRs enhance the intrinsic lysine reactivity of Ube2D3. In the open conformation, Ube2D3-Ub is highly reactive towards free cysteine, but shows greatly reduced reactivity towards free lysine when compared with free Ube2D3-Ub
-
-
-
additional information
?
-
the enzyme interacts with ubiquitin, and E3 ligases of types RING, HECT, and RBR. Neither HECTs nor RBRs enhance the intrinsic lysine reactivity of Ube2D3. In the open conformation, Ube2D3-Ub is highly reactive towards free cysteine, but shows greatly reduced reactivity towards free lysine when compared with free Ube2D3-Ub
-
-
-
additional information
?
-
the enzyme interacts with ubiquitin, and E3 ligases of types RING, HECT, and RBR. Neither HECTs nor RBRs enhance the intrinsic lysine reactivity of Ube2D3. In the open conformation, Ube2D3-Ub is highly reactive towards free cysteine, but shows greatly reduced reactivity towards free lysine when compared with free Ube2D3-Ub
-
-
-
additional information
?
-
the enzyme interacts with ubiquitin, and E3 ligases of types RING, HECT, and RBR. Neither HECTs nor RBRs enhance the intrinsic lysine reactivity of Ube2D3. In the open conformation, Ube2D3-Ub is highly reactive towards free cysteine, but shows greatly reduced reactivity towards free lysine when compared with free Ube2D3-Ub
-
-
-
additional information
?
-
the enzyme interacts with ubiquitin, and E3 ligases of types RING, HECT, and RBR. Neither HECTs nor RBRs enhance the intrinsic lysine reactivity of Ube2D3. In the open conformation, Ube2D3-Ub is highly reactive towards free cysteine, but shows greatly reduced reactivity towards free lysine when compared with free Ube2D3-Ub
-
-
-
additional information
?
-
the enzyme interacts with ubiquitin, and E3 ligases of types RING, HECT, and RBR. Neither HECTs nor RBRs enhance the intrinsic lysine reactivity of Ube2D3. In the open conformation, Ube2D3-Ub is highly reactive towards free cysteine, but shows greatly reduced reactivity towards free lysine when compared with free Ube2D3-Ub
-
-
-
additional information
?
-
the enzyme interacts with ubiquitin, and E3 ligases of types RING, HECT, and RBR. Neither HECTs nor RBRs enhance the intrinsic lysine reactivity of Ube2D3. In the open conformation, Ube2D3-Ub is highly reactive towards free cysteine, but shows greatly reduced reactivity towards free lysine when compared with free Ube2D3-Ub
-
-
-
additional information
?
-
the enzyme interacts with ubiquitin, and E3 ligases of types RING, HECT, and RBR. Neither HECTs nor RBRs enhance the intrinsic lysine reactivity of Ube2D3. In the open conformation, Ube2D3-Ub is highly reactive towards free cysteine, but shows greatly reduced reactivity towards free lysine when compared with free Ube2D3-Ub
-
-
-
additional information
?
-
the enzyme interacts with ubiquitin, and E3 ligases of types RING, HECT, and RBR. Neither HECTs nor RBRs enhance the intrinsic lysine reactivity of Ube2D3. In the open conformation, Ube2D3-Ub is highly reactive towards free cysteine, but shows greatly reduced reactivity towards free lysine when compared with free Ube2D3-Ub
-
-
-
additional information
?
-
the enzyme interacts with ubiquitin, and E3 ligases of types RING, HECT, and RBR. Neither HECTs nor RBRs enhance the intrinsic lysine reactivity of Ube2D3. In the open conformation, Ube2D3-Ub is highly reactive towards free cysteine, but shows greatly reduced reactivity towards free lysine when compared with free Ube2D3-Ub
-
-
-
additional information
?
-
the enzyme interacts with ubiquitin, and E3 ligases of types RING, HECT, and RBR. Neither HECTs nor RBRs enhance the intrinsic lysine reactivity of Ube2D3. In the open conformation, Ube2D3-Ub is highly reactive towards free cysteine, but shows greatly reduced reactivity towards free lysine when compared with free Ube2D3-Ub
-
-
-
additional information
?
-
the enzyme interacts with ubiquitin, and E3 ligases of types RING, HECT, and RBR. Neither HECTs nor RBRs enhance the intrinsic lysine reactivity of Ube2D3. In the open conformation, Ube2D3-Ub is highly reactive towards free cysteine, but shows greatly reduced reactivity towards free lysine when compared with free Ube2D3-Ub
-
-
-
additional information
?
-
the enzyme interacts with ubiquitin, and E3 ligases of types RING, HECT, and RBR. Neither HECTs nor RBRs enhance the intrinsic lysine reactivity of Ube2D3. In the open conformation, Ube2D3-Ub is highly reactive towards free cysteine, but shows greatly reduced reactivity towards free lysine when compared with free Ube2D3-Ub
-
-
-
additional information
?
-
the enzyme interacts with ubiquitin, and E3 ligases of types RING, HECT, and RBR. Neither HECTs nor RBRs enhance the intrinsic lysine reactivity of Ube2D3. In the open conformation, Ube2D3-Ub is highly reactive towards free cysteine, but shows greatly reduced reactivity towards free lysine when compared with free Ube2D3-Ub
-
-
-
additional information
?
-
the enzyme interacts with ubiquitin, and E3 ligases of types RING, HECT, and RBR. Neither HECTs nor RBRs enhance the intrinsic lysine reactivity of Ube2D3. In the open conformation, Ube2D3-Ub is highly reactive towards free cysteine, but shows greatly reduced reactivity towards free lysine when compared with free Ube2D3-Ub
-
-
-
additional information
?
-
the enzyme interacts with ubiquitin, and E3 ligases of types RING, HECT, and RBR. Neither HECTs nor RBRs enhance the intrinsic lysine reactivity of Ube2D3. In the open conformation, Ube2D3-Ub is highly reactive towards free cysteine, but shows greatly reduced reactivity towards free lysine when compared with free Ube2D3-Ub
-
-
-
additional information
?
-
the enzyme interacts with ubiquitin, and E3 ligases of types RING, HECT, and RBR. Neither HECTs nor RBRs enhance the intrinsic lysine reactivity of Ube2D3. In the open conformation, Ube2D3-Ub is highly reactive towards free cysteine, but shows greatly reduced reactivity towards free lysine when compared with free Ube2D3-Ub
-
-
-
additional information
?
-
the enzyme interacts with ubiquitin, and E3 ligases of types RING, HECT, and RBR. Neither HECTs nor RBRs enhance the intrinsic lysine reactivity of Ube2D3. In the open conformation, Ube2D3-Ub is highly reactive towards free cysteine, but shows greatly reduced reactivity towards free lysine when compared with free Ube2D3-Ub
-
-
-
additional information
?
-
the enzyme interacts with ubiquitin, E3 ligases of types RING, HECT, and RBR, with Cue1, and with itself. UBE2G2 is a K48 chain-building enzyme dependent on E3. Chain building directly on E2 active sites has been reported in limited cases (e.g. Ube2G2, and Ube2D in collaboration with the bacterial effector SspH2)
-
-
-
additional information
?
-
the enzyme interacts with ubiquitin, E3 ligases of types RING, HECT, and RBR, with Cue1, and with itself. UBE2G2 is a K48 chain-building enzyme dependent on E3. Chain building directly on E2 active sites has been reported in limited cases (e.g. Ube2G2, and Ube2D in collaboration with the bacterial effector SspH2)
-
-
-
additional information
?
-
the enzyme interacts with ubiquitin, E3 ligases of types RING, HECT, and RBR, with Cue1, and with itself. UBE2G2 is a K48 chain-building enzyme dependent on E3. Chain building directly on E2 active sites has been reported in limited cases (e.g. Ube2G2, and Ube2D in collaboration with the bacterial effector SspH2)
-
-
-
additional information
?
-
the enzyme interacts with ubiquitin, E3 ligases of types RING, HECT, and RBR, with Cue1, and with itself. UBE2G2 is a K48 chain-building enzyme dependent on E3. Chain building directly on E2 active sites has been reported in limited cases (e.g. Ube2G2, and Ube2D in collaboration with the bacterial effector SspH2)
-
-
-
additional information
?
-
the enzyme interacts with ubiquitin, E3 ligases of types RING, HECT, and RBR, with Cue1, and with itself. UBE2G2 is a K48 chain-building enzyme dependent on E3. Chain building directly on E2 active sites has been reported in limited cases (e.g. Ube2G2, and Ube2D in collaboration with the bacterial effector SspH2)
-
-
-
additional information
?
-
the enzyme interacts with ubiquitin, E3 ligases of types RING, HECT, and RBR, with Cue1, and with itself. UBE2G2 is a K48 chain-building enzyme dependent on E3. Chain building directly on E2 active sites has been reported in limited cases (e.g. Ube2G2, and Ube2D in collaboration with the bacterial effector SspH2)
-
-
-
additional information
?
-
the enzyme interacts with ubiquitin, E3 ligases of types RING, HECT, and RBR, with Cue1, and with itself. UBE2G2 is a K48 chain-building enzyme dependent on E3. Chain building directly on E2 active sites has been reported in limited cases (e.g. Ube2G2, and Ube2D in collaboration with the bacterial effector SspH2)
-
-
-
additional information
?
-
the enzyme interacts with ubiquitin, E3 ligases of types RING, HECT, and RBR, with Cue1, and with itself. UBE2G2 is a K48 chain-building enzyme dependent on E3. Chain building directly on E2 active sites has been reported in limited cases (e.g. Ube2G2, and Ube2D in collaboration with the bacterial effector SspH2)
-
-
-
additional information
?
-
the enzyme interacts with ubiquitin, E3 ligases of types RING, HECT, and RBR, with Cue1, and with itself. UBE2G2 is a K48 chain-building enzyme dependent on E3. Chain building directly on E2 active sites has been reported in limited cases (e.g. Ube2G2, and Ube2D in collaboration with the bacterial effector SspH2)
-
-
-
additional information
?
-
the enzyme interacts with ubiquitin, E3 ligases of types RING, HECT, and RBR, with Cue1, and with itself. UBE2G2 is a K48 chain-building enzyme dependent on E3. Chain building directly on E2 active sites has been reported in limited cases (e.g. Ube2G2, and Ube2D in collaboration with the bacterial effector SspH2)
-
-
-
additional information
?
-
the enzyme interacts with ubiquitin, E3 ligases of types RING, HECT, and RBR, with Cue1, and with itself. UBE2G2 is a K48 chain-building enzyme dependent on E3. Chain building directly on E2 active sites has been reported in limited cases (e.g. Ube2G2, and Ube2D in collaboration with the bacterial effector SspH2)
-
-
-
additional information
?
-
the enzyme interacts with ubiquitin, E3 ligases of types RING, HECT, and RBR, with Cue1, and with itself. UBE2G2 is a K48 chain-building enzyme dependent on E3. Chain building directly on E2 active sites has been reported in limited cases (e.g. Ube2G2, and Ube2D in collaboration with the bacterial effector SspH2)
-
-
-
additional information
?
-
the enzyme interacts with ubiquitin, E3 ligases of types RING, HECT, and RBR, with Cue1, and with itself. UBE2G2 is a K48 chain-building enzyme dependent on E3. Chain building directly on E2 active sites has been reported in limited cases (e.g. Ube2G2, and Ube2D in collaboration with the bacterial effector SspH2)
-
-
-
additional information
?
-
the enzyme interacts with ubiquitin, E3 ligases of types RING, HECT, and RBR, with Cue1, and with itself. UBE2G2 is a K48 chain-building enzyme dependent on E3. Chain building directly on E2 active sites has been reported in limited cases (e.g. Ube2G2, and Ube2D in collaboration with the bacterial effector SspH2)
-
-
-
additional information
?
-
the enzyme interacts with ubiquitin, E3 ligases of types RING, HECT, and RBR, with Cue1, and with itself. UBE2G2 is a K48 chain-building enzyme dependent on E3. Chain building directly on E2 active sites has been reported in limited cases (e.g. Ube2G2, and Ube2D in collaboration with the bacterial effector SspH2)
-
-
-
additional information
?
-
the enzyme interacts with ubiquitin, E3 ligases of types RING, HECT, and RBR, with Cue1, and with itself. UBE2G2 is a K48 chain-building enzyme dependent on E3. Chain building directly on E2 active sites has been reported in limited cases (e.g. Ube2G2, and Ube2D in collaboration with the bacterial effector SspH2)
-
-
-
additional information
?
-
the enzyme interacts with ubiquitin, E3 ligases of types RING, HECT, and RBR, with Cue1, and with itself. UBE2G2 is a K48 chain-building enzyme dependent on E3. Chain building directly on E2 active sites has been reported in limited cases (e.g. Ube2G2, and Ube2D in collaboration with the bacterial effector SspH2)
-
-
-
additional information
?
-
the enzyme interacts with ubiquitin, E3 ligases of types RING, HECT, and RBR, with Cue1, and with itself. UBE2G2 is a K48 chain-building enzyme dependent on E3. Chain building directly on E2 active sites has been reported in limited cases (e.g. Ube2G2, and Ube2D in collaboration with the bacterial effector SspH2)
-
-
-
additional information
?
-
the enzyme interacts with ubiquitin, E3 ligases of types RING, HECT, and RBR, with Cue1, and with itself. UBE2G2 is a K48 chain-building enzyme dependent on E3. Chain building directly on E2 active sites has been reported in limited cases (e.g. Ube2G2, and Ube2D in collaboration with the bacterial effector SspH2)
-
-
-
additional information
?
-
the enzyme interacts with ubiquitin, E3 ligases of types RING, HECT, and RBR, with Cue1, and with itself. UBE2G2 is a K48 chain-building enzyme dependent on E3. Chain building directly on E2 active sites has been reported in limited cases (e.g. Ube2G2, and Ube2D in collaboration with the bacterial effector SspH2)
-
-
-
additional information
?
-
the enzyme interacts with ubiquitin, E3 ligases of types RING, HECT, and RBR, with Cue1, and with itself. UBE2G2 is a K48 chain-building enzyme dependent on E3. Chain building directly on E2 active sites has been reported in limited cases (e.g. Ube2G2, and Ube2D in collaboration with the bacterial effector SspH2)
-
-
-
additional information
?
-
the enzyme interacts with ubiquitin, E3 ligases of types RING, HECT, and RBR, with Cue1, and with itself. UBE2G2 is a K48 chain-building enzyme dependent on E3. Chain building directly on E2 active sites has been reported in limited cases (e.g. Ube2G2, and Ube2D in collaboration with the bacterial effector SspH2)
-
-
-
additional information
?
-
the enzyme interacts with ubiquitin, E3 ligases of types RING, HECT, and RBR, with Cue1, and with itself. UBE2G2 is a K48 chain-building enzyme dependent on E3. Chain building directly on E2 active sites has been reported in limited cases (e.g. Ube2G2, and Ube2D in collaboration with the bacterial effector SspH2)
-
-
-
additional information
?
-
the enzyme interacts with ubiquitin, E3 ligases of types RING, HECT, and RBR, with Cue1, and with itself. UBE2G2 is a K48 chain-building enzyme dependent on E3. Chain building directly on E2 active sites has been reported in limited cases (e.g. Ube2G2, and Ube2D in collaboration with the bacterial effector SspH2)
-
-
-
additional information
?
-
the enzyme interacts with ubiquitin, E3 ligases of types RING, HECT, and RBR, with Cue1, and with itself. UBE2G2 is a K48 chain-building enzyme dependent on E3. Chain building directly on E2 active sites has been reported in limited cases (e.g. Ube2G2, and Ube2D in collaboration with the bacterial effector SspH2)
-
-
-
additional information
?
-
the enzyme interacts with ubiquitin, E3 ligases of types RING, HECT, and RBR, with Cue1, and with itself. UBE2G2 is a K48 chain-building enzyme dependent on E3. Chain building directly on E2 active sites has been reported in limited cases (e.g. Ube2G2, and Ube2D in collaboration with the bacterial effector SspH2)
-
-
-
additional information
?
-
the enzyme interacts with ubiquitin, E3 ligases of types RING, HECT, and RBR, with Cue1, and with itself. UBE2G2 is a K48 chain-building enzyme dependent on E3. Chain building directly on E2 active sites has been reported in limited cases (e.g. Ube2G2, and Ube2D in collaboration with the bacterial effector SspH2)
-
-
-
additional information
?
-
the enzyme interacts with ubiquitin, E3 ligases of types RING, HECT, and RBR, with Cue1, and with itself. UBE2G2 is a K48 chain-building enzyme dependent on E3. Chain building directly on E2 active sites has been reported in limited cases (e.g. Ube2G2, and Ube2D in collaboration with the bacterial effector SspH2)
-
-
-
additional information
?
-
the enzyme interacts with ubiquitin, E3 ligases of types RING, HECT, and RBR, with Cue1, and with itself. UBE2G2 is a K48 chain-building enzyme dependent on E3. Chain building directly on E2 active sites has been reported in limited cases (e.g. Ube2G2, and Ube2D in collaboration with the bacterial effector SspH2)
-
-
-
additional information
?
-
the enzyme interacts with ubiquitin, E3 ligases of types RING, HECT, and RBR, with Cue1, and with itself. UBE2G2 is a K48 chain-building enzyme dependent on E3. Chain building directly on E2 active sites has been reported in limited cases (e.g. Ube2G2, and Ube2D in collaboration with the bacterial effector SspH2)
-
-
-
additional information
?
-
the Ube2R1/2 acidic loop participates in Lys48-specific polyubiquitin chain formation by binding to Skp1-cullin-Fbox (SCF), kinetics
-
-
-
additional information
?
-
the Ube2R1/2 acidic loop participates in Lys48-specific polyubiquitin chain formation by binding to Skp1-cullin-Fbox (SCF), kinetics
-
-
-
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
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
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
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
-
-
-
-
?
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
-
-
-
-
?
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
-
-
-
-
?
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
-
-
-
-
?
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
-
-
-
?
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
A1L167, O00762, O14933, P49427, P49459, P51668, P51965, P60604, P61077, P61086, P61088, P62253, P62256, P62837, P63146, P68036, Q13404, Q15819, Q16763, Q5JXB2, Q5VVX9, Q712K3, Q7Z7E8, Q8N2K1, Q8WVN8, Q969T4, Q96LR5, Q9H832, Q9NPD8, Q9Y385
-
-
-
?
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
-
-
-
?
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
-
-
-
?
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
-
-
-
?
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
-
-
-
?
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
-
-
-
?
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
-
-
-
?
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
-
-
-
?
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
-
-
-
?
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
-
-
-
?
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
-
-
-
?
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
-
-
-
?
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
-
erythrocyte spectrin has a chimeric E2/E3 ubiquitin-conjugating/ligating activity, which is capable of ubiquitinating itself
-
-
?
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
-
the enzyme ubiquitinates the N terminus of substrates
-
-
?
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
K48- and K63-linked ubiquitination
-
-
?
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
-
-
-
?
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
-
-
-
-
?
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
-
-
-
-
?
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
-
-
-
-
?
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
-
-
-
?
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
-
-
-
?
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
-
-
-
-
?
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
-
-
-
-
?
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
-
-
-
-
?
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
METALS and IONS
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
INHIBITOR
ORGANISM
UNIPROT
COMMENTARY
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-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
6-chloro-2,3,4,9-tetrahydro-1H-carbazole-1-carboxamide
i.e. EM02, almost complete inhibition of FANCD2 ubiquination
CC0651
A1L167, O00762, O14933, P49427, P49459, P51668, P51965, P60604, P61077, P61086, P61088, P62253, P62256, P62837, P63146, P68036, Q13404, Q15819, Q16763, Q5JXB2, Q5VVX9, Q712K3, Q7Z7E8, Q8N2K1, Q8WVN8, Q969T4, Q96LR5, Q9H832, Q9NPD8, Q9Y385
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
additional information
allosteric inhibition of the SUMO E2 enzyme Ubc9. Identification of two distinct small molecule fragments that bind to Ubc9 at a site distal from its catalytic cysteine. These fragments and related compounds inhibit SUMO conjugation to the enzyme with IC50 values of 1.9-5.8 mM. Mechanistic and biophysical analyses, coupled with molecular dynamics simulations, point toward ligand-induced rigidification of Ubc9 as a mechanism of inhibition, overview
-
additional information
backside binding by accessory elements of the RING E3 Rad18 inhibits the intrinsic chain-forming activity of Ube2B; enzyme UBE2E1 performs autoubiquitylation, ubiquitylation results in inhibition of E2 activity; the backside-binding element of the E3 AO7 decreases the processivity of chain building by the E2 Ube2D2
-
additional information
backside binding by accessory elements of the RING E3 Rad18 inhibits the intrinsic chain-forming activity of Ube2B; enzyme UBE2E1 performs autoubiquitylation, ubiquitylation results in inhibition of E2 activity; the backside-binding element of the E3 AO7 decreases the processivity of chain building by the E2 Ube2D2
-
additional information
backside binding by accessory elements of the RING E3 Rad18 inhibits the intrinsic chain-forming activity of Ube2B; enzyme UBE2E1 performs autoubiquitylation, ubiquitylation results in inhibition of E2 activity; the backside-binding element of the E3 AO7 decreases the processivity of chain building by the E2 Ube2D2
-
additional information
backside binding by accessory elements of the RING E3 Rad18 inhibits the intrinsic chain-forming activity of Ube2B; enzyme UBE2E1 performs autoubiquitylation, ubiquitylation results in inhibition of E2 activity; the backside-binding element of the E3 AO7 decreases the processivity of chain building by the E2 Ube2D2
-
additional information
backside binding by accessory elements of the RING E3 Rad18 inhibits the intrinsic chain-forming activity of Ube2B; enzyme UBE2E1 performs autoubiquitylation, ubiquitylation results in inhibition of E2 activity; the backside-binding element of the E3 AO7 decreases the processivity of chain building by the E2 Ube2D2
-
additional information
backside binding by accessory elements of the RING E3 Rad18 inhibits the intrinsic chain-forming activity of Ube2B; enzyme UBE2E1 performs autoubiquitylation, ubiquitylation results in inhibition of E2 activity; the backside-binding element of the E3 AO7 decreases the processivity of chain building by the E2 Ube2D2
-
additional information
backside binding by accessory elements of the RING E3 Rad18 inhibits the intrinsic chain-forming activity of Ube2B; enzyme UBE2E1 performs autoubiquitylation, ubiquitylation results in inhibition of E2 activity; the backside-binding element of the E3 AO7 decreases the processivity of chain building by the E2 Ube2D2
-
additional information
backside binding by accessory elements of the RING E3 Rad18 inhibits the intrinsic chain-forming activity of Ube2B; enzyme UBE2E1 performs autoubiquitylation, ubiquitylation results in inhibition of E2 activity; the backside-binding element of the E3 AO7 decreases the processivity of chain building by the E2 Ube2D2
-
additional information
backside binding by accessory elements of the RING E3 Rad18 inhibits the intrinsic chain-forming activity of Ube2B; enzyme UBE2E1 performs autoubiquitylation, ubiquitylation results in inhibition of E2 activity; the backside-binding element of the E3 AO7 decreases the processivity of chain building by the E2 Ube2D2
-
additional information
backside binding by accessory elements of the RING E3 Rad18 inhibits the intrinsic chain-forming activity of Ube2B; enzyme UBE2E1 performs autoubiquitylation, ubiquitylation results in inhibition of E2 activity; the backside-binding element of the E3 AO7 decreases the processivity of chain building by the E2 Ube2D2
-
additional information
backside binding by accessory elements of the RING E3 Rad18 inhibits the intrinsic chain-forming activity of Ube2B; enzyme UBE2E1 performs autoubiquitylation, ubiquitylation results in inhibition of E2 activity; the backside-binding element of the E3 AO7 decreases the processivity of chain building by the E2 Ube2D2
-
additional information
backside binding by accessory elements of the RING E3 Rad18 inhibits the intrinsic chain-forming activity of Ube2B; enzyme UBE2E1 performs autoubiquitylation, ubiquitylation results in inhibition of E2 activity; the backside-binding element of the E3 AO7 decreases the processivity of chain building by the E2 Ube2D2
-
additional information
backside binding by accessory elements of the RING E3 Rad18 inhibits the intrinsic chain-forming activity of Ube2B; enzyme UBE2E1 performs autoubiquitylation, ubiquitylation results in inhibition of E2 activity; the backside-binding element of the E3 AO7 decreases the processivity of chain building by the E2 Ube2D2
-
additional information
backside binding by accessory elements of the RING E3 Rad18 inhibits the intrinsic chain-forming activity of Ube2B; enzyme UBE2E1 performs autoubiquitylation, ubiquitylation results in inhibition of E2 activity; the backside-binding element of the E3 AO7 decreases the processivity of chain building by the E2 Ube2D2
-
additional information
backside binding by accessory elements of the RING E3 Rad18 inhibits the intrinsic chain-forming activity of Ube2B; enzyme UBE2E1 performs autoubiquitylation, ubiquitylation results in inhibition of E2 activity; the backside-binding element of the E3 AO7 decreases the processivity of chain building by the E2 Ube2D2
-
additional information
backside binding by accessory elements of the RING E3 Rad18 inhibits the intrinsic chain-forming activity of Ube2B; enzyme UBE2E1 performs autoubiquitylation, ubiquitylation results in inhibition of E2 activity; the backside-binding element of the E3 AO7 decreases the processivity of chain building by the E2 Ube2D2
-
additional information
backside binding by accessory elements of the RING E3 Rad18 inhibits the intrinsic chain-forming activity of Ube2B; enzyme UBE2E1 performs autoubiquitylation, ubiquitylation results in inhibition of E2 activity; the backside-binding element of the E3 AO7 decreases the processivity of chain building by the E2 Ube2D2
-
additional information
backside binding by accessory elements of the RING E3 Rad18 inhibits the intrinsic chain-forming activity of Ube2B; enzyme UBE2E1 performs autoubiquitylation, ubiquitylation results in inhibition of E2 activity; the backside-binding element of the E3 AO7 decreases the processivity of chain building by the E2 Ube2D2
-
additional information
backside binding by accessory elements of the RING E3 Rad18 inhibits the intrinsic chain-forming activity of Ube2B; enzyme UBE2E1 performs autoubiquitylation, ubiquitylation results in inhibition of E2 activity; the backside-binding element of the E3 AO7 decreases the processivity of chain building by the E2 Ube2D2
-
additional information
backside binding by accessory elements of the RING E3 Rad18 inhibits the intrinsic chain-forming activity of Ube2B; enzyme UBE2E1 performs autoubiquitylation, ubiquitylation results in inhibition of E2 activity; the backside-binding element of the E3 AO7 decreases the processivity of chain building by the E2 Ube2D2
-
additional information
backside binding by accessory elements of the RING E3 Rad18 inhibits the intrinsic chain-forming activity of Ube2B; enzyme UBE2E1 performs autoubiquitylation, ubiquitylation results in inhibition of E2 activity; the backside-binding element of the E3 AO7 decreases the processivity of chain building by the E2 Ube2D2
-
additional information
backside binding by accessory elements of the RING E3 Rad18 inhibits the intrinsic chain-forming activity of Ube2B; enzyme UBE2E1 performs autoubiquitylation, ubiquitylation results in inhibition of E2 activity; the backside-binding element of the E3 AO7 decreases the processivity of chain building by the E2 Ube2D2
-
additional information
backside binding by accessory elements of the RING E3 Rad18 inhibits the intrinsic chain-forming activity of Ube2B; enzyme UBE2E1 performs autoubiquitylation, ubiquitylation results in inhibition of E2 activity; the backside-binding element of the E3 AO7 decreases the processivity of chain building by the E2 Ube2D2
-
additional information
backside binding by accessory elements of the RING E3 Rad18 inhibits the intrinsic chain-forming activity of Ube2B; enzyme UBE2E1 performs autoubiquitylation, ubiquitylation results in inhibition of E2 activity; the backside-binding element of the E3 AO7 decreases the processivity of chain building by the E2 Ube2D2
-
additional information
backside binding by accessory elements of the RING E3 Rad18 inhibits the intrinsic chain-forming activity of Ube2B; enzyme UBE2E1 performs autoubiquitylation, ubiquitylation results in inhibition of E2 activity; the backside-binding element of the E3 AO7 decreases the processivity of chain building by the E2 Ube2D2
-
additional information
backside binding by accessory elements of the RING E3 Rad18 inhibits the intrinsic chain-forming activity of Ube2B; enzyme UBE2E1 performs autoubiquitylation, ubiquitylation results in inhibition of E2 activity; the backside-binding element of the E3 AO7 decreases the processivity of chain building by the E2 Ube2D2
-
additional information
backside binding by accessory elements of the RING E3 Rad18 inhibits the intrinsic chain-forming activity of Ube2B; enzyme UBE2E1 performs autoubiquitylation, ubiquitylation results in inhibition of E2 activity; the backside-binding element of the E3 AO7 decreases the processivity of chain building by the E2 Ube2D2
-
additional information
backside binding by accessory elements of the RING E3 Rad18 inhibits the intrinsic chain-forming activity of Ube2B; enzyme UBE2E1 performs autoubiquitylation, ubiquitylation results in inhibition of E2 activity; the backside-binding element of the E3 AO7 decreases the processivity of chain building by the E2 Ube2D2
-
additional information
backside binding by accessory elements of the RING E3 Rad18 inhibits the intrinsic chain-forming activity of Ube2B; enzyme UBE2E1 performs autoubiquitylation, ubiquitylation results in inhibition of E2 activity; the backside-binding element of the E3 AO7 decreases the processivity of chain building by the E2 Ube2D2
-
additional information
backside binding by accessory elements of the RING E3 Rad18 inhibits the intrinsic chain-forming activity of Ube2B; enzyme UBE2E1 performs autoubiquitylation, ubiquitylation results in inhibition of E2 activity; the backside-binding element of the E3 AO7 decreases the processivity of chain building by the E2 Ube2D2
-
additional information
identification of an allosteric pocket on Ube2T through a fragment screening using biophysical methods. Several fragments binding to this site inhibit ubiquitin conjugation in vitro. One-dimensional 1H NMR spectroscopy, binding site identification through protein-observed NMR spectroscopy, and X-ray crystallography, overview. No inhibition by 5-(pyridin-2-yl)thiophene-2-carboxamide (EM29)
-
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ACTIVATING COMPOUND
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
additional information
1,3-bis(2-chloroethyl)-1-nitrosourea (BCNU) and O6-benzylguanine facilitate the ubiquitination and degradation of O6-methylguanine-DNA methyltransferase (MGMT) in several types of cancer cells involving the enzyme ubiquitin-conjugating enzyme E2 B. BCNU enhances the interaction between MGMT and UBE2B
-
additional information
-
1,3-bis(2-chloroethyl)-1-nitrosourea (BCNU) and O6-benzylguanine facilitate the ubiquitination and degradation of O6-methylguanine-DNA methyltransferase (MGMT) in several types of cancer cells involving the enzyme ubiquitin-conjugating enzyme E2 B. BCNU enhances the interaction between MGMT and UBE2B
-
additional information
the ubiquitin-like modifier-activating enzyme 1 (Uba1, EC 6.2.1.45) is a multidomain enzyme that serves as the gatekeeper of the ubiquitin (Ub) conjugation cascade by activating Ub in a two-step process involving adenylation and thioester bond formation followed by transfer of Ub to E2s in a process termed E1-E2 thioester transfer or transthiolation. Cdc34 is one of tens of E2s that must function with Uba1 despite significant differences at their predicted UFD-interacting surfaces. Molecular recognition of Cdc34 by Uba1, overview. Analysis with Uba1 from Homo sapiens, Saccharomyces cerevisiae, and Schizosaccharomyces pombe
-
additional information
Derlin2 interacts with UBC6e in the complex involved in the regulation of ERAD enhancers. Derlin2 levels do not change in UBC6e-/- cells transduced with any of the UBC6e mutants, suggesting that it is not a substrate regulated by UBC6e, but is a member of a UBC6e complex
-
additional information
the ubiquitin-like modifier-activating enzyme 1 (Uba1, EC 6.2.1.45) is a multidomain enzyme that serves as the gatekeeper of the ubiquitin (Ub) conjugation cascade by activating Ub in a two-step process involving adenylation and thioester bond formation followed by transfer of Ub to E2s in a process termed E1-E2 thioester transfer or transthiolation. Cdc34 is one of tens of E2s that must function with Uba1 despite significant differences at their predicted UFD-interacting surfaces. Molecular recognition of Cdc34 by Uba1, overview. Analysis with Uba1 from Homo sapiens, Saccharomyces cerevisiae, and Schizosaccharomyces pombe
-
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KM VALUE [mM]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
1
S-ubiquitinyl-[E1 ubiquitin-activating enzyme]-L-cysteine
about, pH 7.5, temperature not specified in the publication
-
0.000073
[ubiquitin-carrier-protein Ubc2b]-L-cysteine
-
mutant D576N, pH 7.5, temperature not specified in the publication
-
0.000089
[ubiquitin-carrier-protein Ubc2b]-L-cysteine
-
mutant K528A, pH 7.5, temperature not specified in the publication
-
0.000111
[ubiquitin-carrier-protein Ubc2b]-L-cysteine
-
wild-type, pH 7.5, temperature not specified in the publication
-
0.000122
[ubiquitin-carrier-protein Ubc2b]-L-cysteine
-
mutant D576E, pH 7.5, temperature not specified in the publication
-
0.000135
[ubiquitin-carrier-protein Ubc2b]-L-cysteine
-
mutant D576A, pH 7.5, temperature not specified in the publication
-
additional information
additional information
analysis of binding affinity between O6-methylguanine-DNA methyltransferase (MGMT)and E2 ubiquitin conjugating enzymes
-
additional information
additional information
-
analysis of binding affinity between O6-methylguanine-DNA methyltransferase (MGMT)and E2 ubiquitin conjugating enzymes
-
additional information
additional information
initial rates for UBL transfer from the E1 to the E2 enzymes are determined at different E2 concentrations and are fitted using non-linear regression to the Michaelis-Menten model or to a substrate inhibition effect equation. Data, fitted to the Michaelis-Menten model, shows that wild-type UBE2Z, and mutants UBE2ZLB and UBE2ZNter display similar catalytic rates during ubiquitin loading, Enzyme kinetics for UBL loading on UBE2Z variants, overview
-
additional information
additional information
Michaelis constants for wild-type and mutant E2-E3 pairs, E2 is Ube2R2 and E3 is Rbx1, overview
-
additional information
additional information
Michaelis constants for wild-type and mutant E2-E3 pairs, E2 is Ube2R2 and E3 is Rbx1, overview
-
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TURNOVER NUMBER [1/s]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
0.01 - 1
[ubiquitin-carrier-protein Ubc2b]-L-cysteine
-
mutant K528A, pH 7.5, temperature not specified in the publication
-
0.022
[ubiquitin-carrier-protein Ubc2b]-L-cysteine
-
mutant D576N, pH 7.5, temperature not specified in the publication
-
0.1
[ubiquitin-carrier-protein Ubc2b]-L-cysteine
-
mutant D576E, pH 7.5, temperature not specified in the publication
-
0.12
[ubiquitin-carrier-protein Ubc2b]-L-cysteine
-
mutant D576A, pH 7.5, temperature not specified in the publication
-
3.4
[ubiquitin-carrier-protein Ubc2b]-L-cysteine
-
wild-type, pH 7.5, temperature not specified in the publication
-
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IC50 VALUE [mM]
INHIBITOR
ORGANISM
UNIPROT
COMMENTARY
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
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pH OPTIMUM
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
7.5
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TEMPERATURE OPTIMUM
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
37
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ORGANISM
COMMENTARY
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
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SOURCE TISSUE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
SOURCE
quantitative real-time PCR enzyme expression analysis in gastric cancer cell lines, overview
brenda
additional information
-
exclusively expressed in the testis, mainly in the germ cells during the late stage of spermatogenesis, and is localized in the sperm head and tail
brenda
additional information
-
most E2 enzymes have been identified in a wide variety of tissues and cell types
brenda
additional information
-
expression of numerous VvUBCs show significant changes during grapevine development. Expression pattern of VvUBCs in different genotypes, transcriptome analysis, overview
brenda
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LOCALIZATION
ORGANISM
UNIPROT
COMMENTARY
GeneOntology No.
LITERATURE
SOURCE
UBC6e localizes to the ER via its tail-anchor, functional UBC6e requires its precise location in the endoplasmic reticulum to form a supramolecular complex with Derlin2
brenda
additional information
additional information
-
many E2 enzymes are found both in the nucleus and in the cytoplasm. Some E2 enzymes are exclusively restructed to specific compartments
-
brenda
additional information
enzyme UBE2QL1 is diffusely present in the cytosol in untreated cells and translocates to damaged lysosomes
-
brenda
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GENERAL INFORMATION
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
evolution
malfunction
metabolism
physiological function
additional information
evolution
enzyme UBE2L3 belongs to the E2 family. Humans have around 35 ubiquitin E2 family members, all sharing a core ubiquitin conjugation (UBC) domain that spans roughly 150 residues. E2s are classified by their UBC domain extensions, class I E2s have only the core domain, classes II and III have N- or C-terminal extensions respectively, and class IV are extended at both ends
evolution
enzyme UBE2T belongs to the E2 family. Humans have around 35 ubiquitin E2 family members, all sharing a core ubiquitin conjugation (UBC) domain that spans roughly 150 residues. E2s are classified by their UBC domain extensions, class I E2s have only the core domain, classes II and III have N- or C-terminal extensions respectively, and class IV are extended at both ends
evolution
A1L167, O00762, O14933, P49427, P49459, P51668, P51965, P60604, P61077, P61086, P61088, P62253, P62256, P62837, P63146, P68036, Q13404, Q15819, Q16763, Q5JXB2, Q5VVX9, Q712K3, Q7Z7E8, Q8N2K1, Q8WVN8, Q969T4, Q96LR5, Q9H832, Q9NPD8, Q9Y385
humans have about 40 E2s that are involved in the transfer of Ub or Ub-like (Ubl) proteins (e.g. SUMO and NEDD8). Common functional and structural features that define unifying themes among E2s, overview. Highly specific chain builders such as Ube2N, Ube2S, and Ube2R1 can only transfer their conjugated Ub to another Ub molecule. This leads to a division of labor among E2s in which one E2 initiates or primes chain synthesis and a second E2 builds and extends the polyUb chain
evolution
A1L167, O00762, O14933, P49427, P49459, P51668, P51965, P60604, P61077, P61086, P61088, P62253, P62256, P62837, P63146, P68036, Q13404, Q15819, Q16763, Q5JXB2, Q5VVX9, Q712K3, Q7Z7E8, Q8N2K1, Q8WVN8, Q969T4, Q96LR5, Q9H832, Q9NPD8, Q9Y385
humans have about 40 E2s that are involved in the transfer of Ub or Ub-like (Ubl) proteins (e.g., SUMO and NEDD8). Common functional and structural features that define unifying themes among E2s, overview. Highly specific chain builders such as Ube2N, Ube2S, and Ube2R1 can only transfer their conjugated Ub to another Ub molecule. This leads to a division of labor among E2s in which one E2 initiates or primes chain synthesis and a second E2 builds and extends the polyUb chain
evolution
A1L167, O00762, O14933, P49427, P49459, P51668, P51965, P60604, P61077, P61086, P61088, P62253, P62256, P62837, P63146, P68036, Q13404, Q15819, Q16763, Q5JXB2, Q5VVX9, Q712K3, Q7Z7E8, Q8N2K1, Q8WVN8, Q969T4, Q96LR5, Q9H832, Q9NPD8, Q9Y385
humans have about 40 E2s that are involved in the transfer of Ub or Ub-like (Ubl) proteins (e.g., SUMO and NEDD8). Common functional and structural features that define unifying themes among E2s, overview. Highly specific chain builders such as Ube2N, Ube2S, and Ube2R1 can only transfer their conjugated Ub to another Ub molecule. This leads to a division of labor among E2s in which one E2 initiates or primes chain synthesis and a second E2 builds and extends the polyUb chain. Either Ube2C or a Ube2D family member transfers the first Ub onto human APC/C substrates and Ube2S then builds the K11-linked polyUb chains that are a hallmark of APC/C-mediated proteasomal degradation
evolution
-
the enzyme belongs to the E2 gene family, phylogenetic analysis of VvUBC family, 43 VvUBC members can be classified into five groups, expression pattern of VvUBCs in different genotypes, detailed overview. Chromosome localization and gene duplication analysis of VvUBCs
evolution
UBE2Z is a 354-residue-long atypical ubiquitin conjugating enzyme comprising about 100-residue long N- and C-terminal extensions on top of the conserved core UBC domain, classifying it as a class IV E2 enzyme
evolution
ubiquitin-conjugating enzyme E2T (UBE2T) is a member of the E2 family that mediates the ubiquitin-proteasome system and regulates gene expression
malfunction
-
knockdown of E2 enzymes delays ubiquitylation and degradation of mitochondrial substrates like p62 and the adaptor protein p62/SQSTM1. Depletion of UBE2R1 enhances the translocation of Parkin to, and clustering of, mitochondria
malfunction
-
knockdown of enzyme expression in decreases tombusvirus accumulation and reduces symptom severity
malfunction
-
knockdown of enzyme expression in decreases tombusvirus accumulation and reduces symptom severity
malfunction
ablation of UBC6e causes upregulation of active ERAD enhancers and so increases clearance not only of terminally misfolded substrates, but also of wild-type glycoproteins that fold comparatively slowly in vitro and in vivo. The absence of UBC6e increases the levels of ERAD enhancers with a corresponding increase in the rate of clearance of misfolded and/or incompletely folded substrates. UBC6e-/- MEFs show accelerated mannose trimming and premature substrate release from CNX, initiated by ER mannosidase-dependent eviction of substrate from the CNX cycle. Finally, by deletion of UBC6e, accelerated degradation is observed in tissue culture and in vivo, not only for canonical ERAD substrates, but also for folding intermediates of proteins that fold slowly, such as tyrosinase. The UBC6e loss-of-function mutation thus produces a gain-of-function with respect to ERAD activity, overview. Increased degradation of tyrosinase in UBC6e-/- cells and reduced skin tyrosinase levels in UBC6e-/- mice
malfunction
A1L167, O00762, O14933, P49427, P49459, P51668, P51965, P60604, P61077, P61086, P61088, P62253, P62256, P62837, P63146, P68036, Q13404, Q15819, Q16763, Q5JXB2, Q5VVX9, Q712K3, Q7Z7E8, Q8N2K1, Q8WVN8, Q969T4, Q96LR5, Q9H832, Q9NPD8, Q9Y385
backside binding by accessory elements of the RING E3 Rad18 inhibits the intrinsic chain-forming activity of Ube2B, thus promoting monoubiquitylation of PCNA and histone 2B
malfunction
A1L167, O00762, O14933, P49427, P49459, P51668, P51965, P60604, P61077, P61086, P61088, P62253, P62256, P62837, P63146, P68036, Q13404, Q15819, Q16763, Q5JXB2, Q5VVX9, Q712K3, Q7Z7E8, Q8N2K1, Q8WVN8, Q969T4, Q96LR5, Q9H832, Q9NPD8, Q9Y385
Disruption of specific interactions involving K48 on Ub and backside residues of the E2 by mutation of either Ub or E2 backside residues results in the rapid generation of K63-linked Ub chains by Ube2E3
malfunction
in UBE2G2 knockout cells, sterol-stimulated degradation of squalene monooxygenase (SQLE) is partly attenuated, but that of 3-hydroxy-3-methylglutaryl coenzyme A reductase (HMGCR) is abolished
malfunction
in UBE2J1 knockout cells, sterol-stimulated degradation of squalene monooxygenase (SQLE) and of 3-hydroxy-3-methylglutaryl coenzyme A reductase (HMGCR) are unaffected
malfunction
in UBE2J2 knockout cells, sterol-stimulated degradation of squalene monooxygenase (SQLE), but not that of 3-hydroxy-3-methylglutaryl coenzyme A reductase (HMGCR), is largely attenuated. RNAi-mediated silencing of UBE2J2 expression in HepG2 cells also attenuates sterol-stimulated degradation of SQLE in a proteasome-dependent manner
malfunction
knocking down ubiquitin-conjugating enzyme E2 D1 (Ube2D1) impairs March-I ubiquitination, increased March-I expression, and enhanced March-I-dependent down-regulation of MHC-II proteins
malfunction
mutation in UBE2T are involved in the Fanconi anaemia pathway. UBE2T is the E2 enzyme in the Fanconi anaemia pathway, the Fanconi anaemia ubiquitin signalling module. Analysis of E2 function in the Fanconi anaemia syndrome (FA) disease, patient phenotypes, detailed overview
malfunction
A1L167, O00762, O14933, P49427, P49459, P51668, P51965, P60604, P61077, P61086, P61088, P62253, P62256, P62837, P63146, P68036, Q13404, Q15819, Q16763, Q5JXB2, Q5VVX9, Q712K3, Q7Z7E8, Q8N2K1, Q8WVN8, Q969T4, Q96LR5, Q9H832, Q9NPD8, Q9Y385
mutations designed to disrupt canonical E2/RING interactions that would involve the APC/C RING domain subunit (Apc11) do not affect activity
malfunction
overexpression/knockdown of UBE2B enhances/reduces BCNU-mediated O6-methylguanine-DNA methyltransferase (MGMT) ubiquitination. UBE2B knockdown significantly increases 1,3-bis(2-chloroethyl)-1-nitrosourea (BCNU)cytotoxicity in NPC cells. Therefore, loss of UBE2B seems to disrupt ubiquitin-mediated degradation of alkylated MGMT. UBE2B knockdown reduces MGMT activity, suggesting that loss of UBE2B leads to the accumulation of deactivated MGMT and suppresses MGMT protein turnover in BCNU-treated cells
malfunction
UBE2J2 depletion increases TRC8 expression levels in the presence of US2, and in this way, enhances US2-mediated HLA-I downregulation
malfunction
UBE2T downregulation induces gastric cancer cell cycle arrest
malfunction
without this enzyme, the clearance of ruptured lysosomes is compromised not only upon lysosomal damage but also under normal conditions, revealing its adaptive and constitutive functions. Depletion of the E2 enzyme UBE2QL1 successfully inhibits damage-induced lysosomal ubiquitination. UBE2QL1 depletion affection is greater for K48-linked ubiquitination (K48-Ub) than K63-linked ubiquitination (K63-Ub)
malfunction
-
knockdown of enzyme expression in decreases tombusvirus accumulation and reduces symptom severity
-
metabolism
March-I is ubiquitinated and degraded in the endocytic pathway involving enzyme UBE2D2
metabolism
misfolded endoplasmic reticulum (ER) proteins are dislocated towards the cytosol and degraded by the ubiquitin-proteasome system in a process called ER-associated protein degradation (ERAD). During infection with human cytomegalovirus (HCMV), the viral US2 protein targets HLA class I molecules (HLA-I) for degradation via ERAD to avoid elimination by the immune system. US2-mediated degradation of HLA-I serves as a paradigm of ERAD and has facilitated the identification of TRC8 (also known as RNF139) as an E3 ubiquitin ligase. Identification of multiple E2 enzymes that are involved in the US2-mediated HLA-I downregulation process, of which UBE2G2 is crucial for the degradation of various immunoreceptors. UBE2G2 affects US2-mediated degradation of HLA-I
metabolism
misfolded endoplasmic reticulum (ER) proteins are dislocated towards the cytosol and degraded by the ubiquitin-proteasome system in a process called ER-associated protein degradation (ERAD). During infection with human cytomegalovirus (HCMV), the viral US2 protein targets HLA class I molecules (HLA-I) for degradation via ERAD to avoid elimination by the immune system. US2-mediated degradation of HLA-I serves as a paradigm of ERAD and has facilitated the identification of TRC8 (also known as RNF139) as an E3 ubiquitin ligase. Identification of multiple E2 enzymes that are involved in the US2-mediated HLA-I downregulation process. UBE2D3 affects US2-mediated degradation of HLA-I
metabolism
misfolded endoplasmic reticulum (ER) proteins are dislocated towards the cytosol and degraded by the ubiquitin-proteasome system in a process called ER-associated protein degradation (ERAD). During infection with human cytomegalovirus (HCMV), the viral US2 protein targets HLA class I molecules (HLA-I) for degradation via ERAD to avoid elimination by the immune system. US2-mediated degradation of HLA-I serves as a paradigm of ERAD and has facilitated the identification of TRC8 (also known as RNF139) as an E3 ubiquitin ligase. Identification of multiple E2 enzymes that are involved in the US2-mediated HLA-I downregulation process. UBE2J2 counteracts US2-mediated HLA-I downregulation, UBE2J2 counteracts US2-induced ERAD by downregulating TRC8 expression
metabolism
the enzyme is involved in lysophagy induced by lysosomal membrane rupture, pathway overview
metabolism
the enzyme is involved in the ubiquitin pathway. The E1 mediates ubiquitin activation in an energy-consuming step. The ubiquitin thioester is then transferred onto a catalytic cysteine of the E2 enzyme. RING-type E3s form a non-covalent complex with the E2-Ub thioester intermediate or, alternatively, ubiquitin is transferred to catalytic sites of HECT and RBR-type E3 ligases. The E3 enzymes ultimately catalyze ubiquitination of a substrate lysine. Ubiquitin signals can also be extended to form polyubiquitin chains
metabolism
the enzyme UbeC6 is involved in the endoplasmic reticulum (ER) associated degradation (ERAD)
metabolism
the ubiquitin-like modifier-activating enzyme 1 (Uba1, EC 6.2.1.45) is a multidomain enzyme that serves as the gatekeeper of the ubiquitin (Ub) conjugation cascade by activating Ub in a two-step process involving adenylation and thioester bond formation followed by transfer of Ub to E2s in a process termed E1-E2 thioester transfer or transthiolation. Cdc34 is one of tens of E2s that must function with Uba1 despite significant differences at their predicted UFD-interacting surfaces. Molecular recognition of Cdc34 by Uba1, overview
metabolism
the ubiquitin-like modifier-activating enzyme 1 (Uba1, EC 6.2.1.45) is a multidomain enzyme that serves as the gatekeeper of the ubiquitin (Ub) conjugation cascade by activating Ub in a two-step process involving adenylation and thioester bond formation followed by transfer of Ub to E2s in a process termed E1-E2 thioester transfer or transthiolation. Cdc34 is one of tens of E2s that must function with Uba1 despite significant differences at their predicted UFD-interacting surfaces. Molecular recognition of Cdc34 by Uba1, overview
metabolism
Ube2T is the E2 ubiquitin-conjugating enzyme of the Fanconi anemia DNA repair pathway
metabolism
A1L167, O00762, O14933, P49427, P49459, P51668, P51965, P60604, P61077, P61086, P61088, P62253, P62256, P62837, P63146, P68036, Q13404, Q15819, Q16763, Q5JXB2, Q5VVX9, Q712K3, Q7Z7E8, Q8N2K1, Q8WVN8, Q969T4, Q96LR5, Q9H832, Q9NPD8, Q9Y385
ubiquitin-conjugating enzymes (E2s) are the central players in the trio of enzymes responsible for the attachment of ubiquitin (Ub) to cellular proteins
metabolism
A1L167, O00762, O14933, P49427, P49459, P51668, P51965, P60604, P61077, P61086, P61088, P62253, P62256, P62837, P63146, P68036, Q13404, Q15819, Q16763, Q5JXB2, Q5VVX9, Q712K3, Q7Z7E8, Q8N2K1, Q8WVN8, Q969T4, Q96LR5, Q9H832, Q9NPD8, Q9Y385
ubiquitin-conjugating enzymes (E2s) are the central players in the trio of enzymes responsible for the attachment of ubiquitin (Ub) to cellular proteins. E2 enzyme Ube2W (EC 2.3.2.25) can transfer Ub to the alpha-amino group of small lysine-less peptides but not to free lysine, whereas Ube2D3, for example, can transfer Ub to lysine but not to the alpha-amino group
metabolism
A1L167, O00762, O14933, P49427, P49459, P51668, P51965, P60604, P61077, P61086, P61088, P62253, P62256, P62837, P63146, P68036, Q13404, Q15819, Q16763, Q5JXB2, Q5VVX9, Q712K3, Q7Z7E8, Q8N2K1, Q8WVN8, Q969T4, Q96LR5, Q9H832, Q9NPD8, Q9Y385
ubiquitin-conjugating enzymes (E2s) are the central players in the trio of enzymes responsible for the attachment of ubiquitin (Ub) to cellular proteins. E2 regulation mechanisms, overview
metabolism
A1L167, O00762, O14933, P49427, P49459, P51668, P51965, P60604, P61077, P61086, P61088, P62253, P62256, P62837, P63146, P68036, Q13404, Q15819, Q16763, Q5JXB2, Q5VVX9, Q712K3, Q7Z7E8, Q8N2K1, Q8WVN8, Q969T4, Q96LR5, Q9H832, Q9NPD8, Q9Y385
ubiquitin-conjugating enzymes (E2s) are the central players in the trio of enzymes responsible for the attachment of ubiquitin (Ub) to cellular proteins. Either Ube2C or a Ube2D family member transfers the first Ub onto human APC/C substrates and Ube2S then builds the K11-linked polyUb chains that are a hallmark of APC/C-mediated proteasomal degradation. The APC/C appears to repurpose its RING subunit to bind and track the growing Ub chain during Ube2S-mediated catalysis, presumably inhibiting incorrect chain building by the promiscuous Ube2D E2s. E2 regulation mechanisms, overview
metabolism
A1L167, O00762, O14933, P49427, P49459, P51668, P51965, P60604, P61077, P61086, P61088, P62253, P62256, P62837, P63146, P68036, Q13404, Q15819, Q16763, Q5JXB2, Q5VVX9, Q712K3, Q7Z7E8, Q8N2K1, Q8WVN8, Q969T4, Q96LR5, Q9H832, Q9NPD8, Q9Y385
ubiquitin-conjugating enzymes (E2s) are the central players in the trio of enzymes responsible for the attachment of ubiquitin (Ub) to cellular proteins. Enzyme UBE2J1 is involved in the ERAD pathway. E2 regulation mechanisms, overview
metabolism
A1L167, O00762, O14933, P49427, P49459, P51668, P51965, P60604, P61077, P61086, P61088, P62253, P62256, P62837, P63146, P68036, Q13404, Q15819, Q16763, Q5JXB2, Q5VVX9, Q712K3, Q7Z7E8, Q8N2K1, Q8WVN8, Q969T4, Q96LR5, Q9H832, Q9NPD8, Q9Y385
ubiquitin-conjugating enzymes (E2s) are the central players in the trio of enzymes responsible for the attachment of ubiquitin (Ub) to cellular proteins. UBE2G2 is an E2 involved in the ERAD pathway. E2 regulation mechanisms, overview
metabolism
A1L167, O00762, O14933, P49427, P49459, P51668, P51965, P60604, P61077, P61086, P61088, P62253, P62256, P62837, P63146, P68036, Q13404, Q15819, Q16763, Q5JXB2, Q5VVX9, Q712K3, Q7Z7E8, Q8N2K1, Q8WVN8, Q969T4, Q96LR5, Q9H832, Q9NPD8, Q9Y385
ubiquitin-conjugating enzymes (E2s) are the central players in the trio of enzymes responsible for the attachment of ubiquitin (Ub) to cellular proteins. Ube2R1 and its yeast counterpart Cdc34 are dedicated E2s for the large multi-subunit SCF (Skp/Cullin/F-Box) E3s that target proteins to the proteasome for degradation. Both of these enzymes also have an acidic C-terminal extension that interacts with a basic canyon on the cullin subunit of an SCF complex, helping to position the E2 near the RING subunit while allowing for rapid association and turnover in chain building. A disulfide bond formed between the Ub E1 Uba1 and the E2 Ube2R1 upon oxidative stress is associated with increased Ube2R1 substrate stability and delayed cell cycle progression. E2 regulation mechanisms, overview
metabolism
A1L167, O00762, O14933, P49427, P49459, P51668, P51965, P60604, P61077, P61086, P61088, P62253, P62256, P62837, P63146, P68036, Q13404, Q15819, Q16763, Q5JXB2, Q5VVX9, Q712K3, Q7Z7E8, Q8N2K1, Q8WVN8, Q969T4, Q96LR5, Q9H832, Q9NPD8, Q9Y385
ubiquitin-conjugating enzymes (E2s) are the central players in the trio of enzymes responsible for the attachment of ubiquitin (Ub) to cellular proteins. Ube2W (EC 2.3.2.25) appears to monoubiquitylate the RING E3 ligases TRIM5alpha and TRIM21, a prerequisite for their K63 polyubiquitylation by Ube2N/Ube2V2. E2 regulation mechanisms, overview
metabolism
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the ubiquitin-like modifier-activating enzyme 1 (Uba1, EC 6.2.1.45) is a multidomain enzyme that serves as the gatekeeper of the ubiquitin (Ub) conjugation cascade by activating Ub in a two-step process involving adenylation and thioester bond formation followed by transfer of Ub to E2s in a process termed E1-E2 thioester transfer or transthiolation. Cdc34 is one of tens of E2s that must function with Uba1 despite significant differences at their predicted UFD-interacting surfaces. Molecular recognition of Cdc34 by Uba1, overview
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physiological function
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Some E2s possess N and/or C-terminal extensions that mediate E2-specific processes: class I, enzyme consists of the catalytic domain, without extensions, Class II, enzyme has a N-terminal extension, class III, enzyme has a C-terminal extension, class IV, enzyme has both, N- and C-terminal extensions, showing differences in function, subcellular localization, stabilization of the interaction with E1 enzymes, or modulation of the activity of the interacting E3
physiological function
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the family of ubiquitin-conjugating enzymes is characterized by the presence of a highly conserved ubiquitin-conjugating (UBC) domain
physiological function
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ubiquitination is involved in myriad cell and disease pathways. The ubiquitin-conjugating E2 is the central player in the ubiquitin-transfer pathway
physiological function
isoform UBC1 can partially complement the function of the yeast UBC4 and UBC5 genes. UBC1 overexpressing Vigna radiata plants display highly sensitive responses to abscisic acid and osmotic stress during germination, enhanced abscisc acid- or salt-induced stomatal closing, and increased drought stress tolerance. The expression levels of a number of key abscisic acid signaling genes are increased in overexpressing plants. Protein UBC1 interacts with a C3HC4-type RING E3 ligase named VBP1, i.e. VrUBC1 Binding Partner 1
physiological function
lack of isoform Ubc2 expression leads to a slightly enhanced resistance level against Pto DC3000 pathogen inoculation
physiological function
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silencing of isoform Ubc2 expression by 77% does not affect the level of resistance against avirulent Pto DC3000 strain inoculation. Silencing leads to upregulation of diesease-related genes RAR1 and SGT1 whereas the expression level of HSP90 only slightly increases
physiological function
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ubiquitin-conjugating enzyme UbcM2 is a regulator of transcription factor nuclear factor E2-related factor Nrf2. Nrf2 induces the expression of antioxidant gene products that neutralize reactive oxygen species and restore redox homeostasis Recombinant Nrf2 and UbcM2 form a complex upon alkylation of a non-catalytic cysteine in UbcM2, Cys-136. UbcM2 and Nrf2 form a nuclear complex utilizing the DNA binding Neh1 domain of Nrf2. UbcM2 can enhance the transcriptional activity of endogenous Nrf2 and Cys-136 and the active-site cysteine, Cys-145, jointly contribute to this regulation
physiological function
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E2 ubiquitin conjugating enzymes UBE2D1, UBE2D2, UBE2D3, UBE2D4, UBE2E1, UBE2E2, UBE2E3 and UBE2N interact non-hierarchically and exclusively with deubiquitylating enzyme OTUB1, i.e. Otubain-1
physiological function
HECT-E3 ligase ETC-1 ubiquitylates securin IFY-1 and cyclin B1 in the presence of the E2 enzyme UBC-18, which functions in pharyngeal development. UBC-18 plays a distinct role together with ETC-1 in regulating the cytoplasmic level of IFY-1 during meiosis
physiological function
isoform TRIP12 catalyzes in vitro ubiquitination of ubiquitin fusion degradation substrates in conjunction with E1, E2, and E4 enzymes. Knockdown of TRIP12 stabilizes artificial ubiquitin fusion degradation substrates and physiological substrate, mutant ubiquitin UBB+1. TRIP12 knockdown reduces UBB+1-induced cell death in human neuroblastoma cells. Complementation of TRIP12 knockdown cells with the TRIP12 HECT domain mostly restores efficient degradation of ubiquitin fusion degradation substrates. The TRIP12 HECT domain directs ubiquitination of ubiquitin fusion degradation substrates in vitro and can be specifically cross-linked to the ubiquitin moiety of the substrates in vivo. A mutant ubiquitin that cannot be conjugated to other proteins is a substrate of the TRIP12 HECT domain both in vivo and in vitro
physiological function
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reduction of Ubc9 protein levels by small interfering RNA attenuates hormonal activation of a mineralocorticoid receptor reporter construct as well as an endogenous target gene by mineralocorticoid receptor. A sumoylation-inactive mutant Ubc9 (C93S) similarly interacts with mineralocorticoid receptor and potentiates aldosterone-dependent mineralocorticoid receptor transactivation. An mineralocorticoid receptor mutant in which four lysine residues within sumoylation motifs are mutated into arginine (K89R/K399R/K494R/K953R) fails to be sumoylated, but Ubc9 similarly enhances transactivation by the mutant mineralocorticoid receptor. Coexpression of Ubc9 and steroid receptor coactivator SRC-1 synergistically enhances mineralocorticoid receptor-mediated transactivation in transient transfection assays
physiological function
residues within helix alpha2 of Ubc7 that interact with donor ubiquitin are essential for polyubiquitin conjugation by Ubc7 and its cognate E3 enzymes. Mutagenesis of these residues inhibits the in vitro activity of Ubc7 by preventing the conjugation of donor ubiquitin to the acceptor. Ubiquitin chain formation by mutant Ubc7 is restored selectively by the E3 enzyme Hrd1 RING domain but not by the E3 enzyme Doa10 RING domain. alpha2 Helix mutations selectively impair the in vivo degradation of Doa10 substrates but have no apparent effect on the degradation of Hrd1 substrates
physiological function
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the cognate E2 coenzymes of E3 enzyme Parkin regulate the activation, translocation and enzymatic functions of Parkin during mitochondrial quality control. UBE2D family members and UBE2L3 redundantly charge the RING-HECT hybrid ligase Parkin with ubiquitin, resulting in its initial activation and translocation to mitochondria. UBE2N primarily mediates the proper clustering of mitochondria, a prerequisite for degradation. Depletion of UBE2R1 results in enhanced Parkin translocation and clustering upon mitochondrial uncoupling
physiological function
Ubc11 gene encodes one of the two E2 enzymes required for progression through mitosis in fission yeast
physiological function
Ubc13 null mutant lines in which the two Ubc13 genes are disrupted display altered root development, including shorter primary root, fewer lateral roots and only a few short root hairs in comparison with the wild type and single mutant plants. The double mutant plants are insensitive to auxin treatments. Instead, the Ubc13 mutant has a reduced auxin response. Both the enzymatic activity and protein level of an AXR3/IAA17-GUS reporter are greatly increased in the Ubc13 mutant, whereas the induction of many auxin-responsive genes is suppressed
physiological function
Ube2J1-/- mice have reduced viability and fail to thrive early after birth. Male Ube2J1-/- mice are sterile due to a defect in late spermatogenesis. Removal of the cytoplasm is incomplete in Ube2J1-/- elongating spermatids, compromising the release of mature elongate spermatids into the lumen of the seminiferous tubule
physiological function
USE1 modifies itself with HLA-F adjacent transcript 10, i.e. FAT10, in cis, mainly at Lys323. Mutation of Lys323 to an arginine does not abolish auto-FAT10ylation of USE1, but every other lysine can instead be modified with FAT10. FAT10ylation of USE1 accelerates its proteasomal degradation. The USE1FAT10 conjugate continues to be an active E2 enzyme
physiological function
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E2 enzymes regulate activation and mitochondrial translocation of Parkin. UBE2L3 is able to charge Parkin with ubiquitin and are essential for its initial activation
physiological function
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the enzyme is correlated with the cryogenic autolysis of Volvariella volvacea
physiological function
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the enzyme is critical for tombvirus replication and is involved in promoting the subversion of Vps23p and Vps4p ESCRT proteins for viral replicase complex assembly
physiological function
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the enzyme is critical for tombvirus replication and is involved in promoting the subversion of Vps23p and Vps4p ESCRT proteins for viral replicase complex assembly
physiological function
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the enzyme plays an important role in the innate immunity of Solanum peruvianum against Clavibacter michiganensis subsp. michiganensis
physiological function
study on energy landscapes during the initial phases of the ubiquitination reaction, on Ube2g2 in the free form and in complex with E3 enzyme gp78 domains RING and G2BR. Ube2g2 goes through a sequence of allosteric binding to gp78, transfer of Ub, and release from gp78 during the ubiquitination reaction. Ube2g2 dynamics is significantly modulated along this pathway, and the population distribution in the dynamic energy landscape drives the sequence of allosteric binding, catalysis and release
physiological function
although damaged lysosomes with ruptured membranes can be repaired, these dangerous organelles are also selectively eliminated by autophagic degradation termed lysophagy. This process is initiated by ubiquitination of lysosomal proteins. The E2 enzyme UBE2QL1 catalyzes ubiquitination of damaged lysosomes. UBE2QL1-mediated ubiquitination of lysosomal proteins is crucial for lysophagy following various types of lysosomal damage. L-leucyl-L-leucine methyl ester (LLOMe) treatment induces both ubiquitin K48- and K63-linked ubiquitination through damage of lysosomal membranes. UBE2QL1 has a constitutive housekeeping role in lysosomal homeostasis. UBE2QL1-dependent ubiquitination recruits VCP and SQSTM1 and induces autophagosome formation. Identification of lysosomal membrane proteins, including LIMP2, NPC1, LAMP1, and LAMP2, as potential targets of ubiquitination. UBE2QL1 itself might recognize membrane pores of damaged lysosomes or it might be recruited by an E3 enzyme
physiological function
enzyme UBE2T promotes cell proliferation and inhibits cell cycle arrest. In addition, UBE2T modulates cell mobility by inducing epithelial-mesenchymal transition. UBE2T plays an important role in the tumorigenesis of gastric cancer, it promotes tumor cell growth and metastasis. UBE2T has been reported to be recruited independently to regulate FANCD2 monoubiquitination and participates in the Fanconi anemia pathway together with FANCD2
physiological function
A1L167, O00762, O14933, P49427, P49459, P51668, P51965, P60604, P61077, P61086, P61088, P62253, P62256, P62837, P63146, P68036, Q13404, Q15819, Q16763, Q5JXB2, Q5VVX9, Q712K3, Q7Z7E8, Q8N2K1, Q8WVN8, Q969T4, Q96LR5, Q9H832, Q9NPD8, Q9Y385
humans have about 40 E2s that are involved in the transfer of Ub or Ub-like (Ubl) proteins (e.g. SUMO and NEDD8). Although the majority of E2s are only twice the size of Ub, this remarkable family of enzymes performs a variety of functional roles
physiological function
A1L167, O00762, O14933, P49427, P49459, P51668, P51965, P60604, P61077, P61086, P61088, P62253, P62256, P62837, P63146, P68036, Q13404, Q15819, Q16763, Q5JXB2, Q5VVX9, Q712K3, Q7Z7E8, Q8N2K1, Q8WVN8, Q969T4, Q96LR5, Q9H832, Q9NPD8, Q9Y385
humans have about 40 E2s that are involved in the transfer of Ub or Ub-like (Ubl) proteins (e.g. SUMO and NEDD8). Although the majority of E2s are only twice the size of Ub, this remarkable family of enzymes performs a variety of functional roles. Enzyme Ube2D1 is a promiscuous lysine- and cysteine-reactive E2
physiological function
A1L167, O00762, O14933, P49427, P49459, P51668, P51965, P60604, P61077, P61086, P61088, P62253, P62256, P62837, P63146, P68036, Q13404, Q15819, Q16763, Q5JXB2, Q5VVX9, Q712K3, Q7Z7E8, Q8N2K1, Q8WVN8, Q969T4, Q96LR5, Q9H832, Q9NPD8, Q9Y385
humans have about 40 E2s that are involved in the transfer of Ub or Ub-like (Ubl) proteins (e.g. SUMO and NEDD8). Although the majority of E2s are only twice the size of Ub, this remarkable family of enzymes performs a variety of functional roles. Enzyme Ube2D3 is a promiscuous lysine- and cysteine-reactive E2
physiological function
A1L167, O00762, O14933, P49427, P49459, P51668, P51965, P60604, P61077, P61086, P61088, P62253, P62256, P62837, P63146, P68036, Q13404, Q15819, Q16763, Q5JXB2, Q5VVX9, Q712K3, Q7Z7E8, Q8N2K1, Q8WVN8, Q969T4, Q96LR5, Q9H832, Q9NPD8, Q9Y385
humans have about 40 E2s that are involved in the transfer of Ub or Ub-like (Ubl) proteins (e.g. SUMO and NEDD8). Although the majority of E2s are only twice the size of Ub, this remarkable family of enzymes performs a variety of functional roles. Enzyme Ube2D4 is a promiscuous lysine- and cysteine-reactive E2
physiological function
A1L167, O00762, O14933, P49427, P49459, P51668, P51965, P60604, P61077, P61086, P61088, P62253, P62256, P62837, P63146, P68036, Q13404, Q15819, Q16763, Q5JXB2, Q5VVX9, Q712K3, Q7Z7E8, Q8N2K1, Q8WVN8, Q969T4, Q96LR5, Q9H832, Q9NPD8, Q9Y385
humans have about 40 E2s that are involved in the transfer of Ub or Ub-like (Ubl) proteins (e.g. SUMO and NEDD8). Although the majority of E2s are only twice the size of Ub, this remarkable family of enzymes performs a variety of functional roles. Enzyme UBE2E1 is a monoubiquitylating E2 of its N-terminal extension
physiological function
A1L167, O00762, O14933, P49427, P49459, P51668, P51965, P60604, P61077, P61086, P61088, P62253, P62256, P62837, P63146, P68036, Q13404, Q15819, Q16763, Q5JXB2, Q5VVX9, Q712K3, Q7Z7E8, Q8N2K1, Q8WVN8, Q969T4, Q96LR5, Q9H832, Q9NPD8, Q9Y385
humans have about 40 E2s that are involved in the transfer of Ub or Ub-like (Ubl) proteins (e.g. SUMO and NEDD8). Although the majority of E2s are only twice the size of Ub, this remarkable family of enzymes performs a variety of functional roles. Enzyme UBE2E1 is a monoubiquitylating E2 of its N-terminal extension. The E2 Ube2E3 regulates the activity of Nrf2, a transcription factor that induces expression of anti-oxidant genes to neutralize reactive oxygen species and restore redox homeostasis. Alkylation of non-catalytic C136 of Ube2E3 (to mimic its oxidation) results in constitutive binding of the E2 to Nrf2, increasing its half-life and thus its transcriptional activity. The regulation also depends on the catalytic activity of Ube2E3. Intriguingly, Ube2E3's C136 replaces the proline in a conserved HPN triad, which has been reported to be required for E2 activity
physiological function
A1L167, O00762, O14933, P49427, P49459, P51668, P51965, P60604, P61077, P61086, P61088, P62253, P62256, P62837, P63146, P68036, Q13404, Q15819, Q16763, Q5JXB2, Q5VVX9, Q712K3, Q7Z7E8, Q8N2K1, Q8WVN8, Q969T4, Q96LR5, Q9H832, Q9NPD8, Q9Y385
humans have about 40 E2s that are involved in the transfer of Ub or Ub-like (Ubl) proteins (e.g. SUMO and NEDD8). Although the majority of E2s are only twice the size of Ub, this remarkable family of enzymes performs a variety of functional roles. Enzyme UBE2E2 is a monoubiquitylating E2 by of its N-terminal extension
physiological function
A1L167, O00762, O14933, P49427, P49459, P51668, P51965, P60604, P61077, P61086, P61088, P62253, P62256, P62837, P63146, P68036, Q13404, Q15819, Q16763, Q5JXB2, Q5VVX9, Q712K3, Q7Z7E8, Q8N2K1, Q8WVN8, Q969T4, Q96LR5, Q9H832, Q9NPD8, Q9Y385
humans have about 40 E2s that are involved in the transfer of Ub or Ub-like (Ubl) proteins (e.g. SUMO and NEDD8). Although the majority of E2s are only twice the size of Ub, this remarkable family of enzymes performs a variety of functional roles. Enzyme UBE2N is collaborating with proteins of the Ube2V family to build K63 Ub-chain. Ube2W (EC 2.3.2.25) appears to monoubiquitylate the RING E3 ligases TRIM5alpha and TRIM21, a prerequisite for their K63 polyubiquitylation by Ube2N/Ube2V2, Ube2N/Ube2V2 form a E2/E3 pair
physiological function
A1L167, O00762, O14933, P49427, P49459, P51668, P51965, P60604, P61077, P61086, P61088, P62253, P62256, P62837, P63146, P68036, Q13404, Q15819, Q16763, Q5JXB2, Q5VVX9, Q712K3, Q7Z7E8, Q8N2K1, Q8WVN8, Q969T4, Q96LR5, Q9H832, Q9NPD8, Q9Y385
humans have about 40 E2s that are involved in the transfer of Ub or Ub-like (Ubl) proteins (e.g. SUMO and NEDD8). Although the majority of E2s are only twice the size of Ub, this remarkable family of enzymes performs a variety of functional roles. Enzymes UBE2V1, UBE2V2, and homologues are catalytically inactive E2-like proteins interacting with Ube2N for K63 chain formation
physiological function
A1L167, O00762, O14933, P49427, P49459, P51668, P51965, P60604, P61077, P61086, P61088, P62253, P62256, P62837, P63146, P68036, Q13404, Q15819, Q16763, Q5JXB2, Q5VVX9, Q712K3, Q7Z7E8, Q8N2K1, Q8WVN8, Q969T4, Q96LR5, Q9H832, Q9NPD8, Q9Y385
humans have about 40 E2s that are involved in the transfer of Ub or Ub-like (Ubl) proteins (e.g. SUMO and NEDD8). Although the majority of E2s are only twice the size of Ub, this remarkable family of enzymes performs a variety of functional roles. Enzymes UBE2V1, UBE2V2, and homologues are catalytically inactive E2-like proteins interacting with Ube2N for K63 chain formation. PCNA is monoubiquitylated by the E2/E3 pair Ube2N/Ube2V2 and the RING E3 Rad5, together builds a K63-linked chain at the same site, to create a signal that promotes template-switching and engagement of the homologous recombination machinery
physiological function
A1L167, O00762, O14933, P49427, P49459, P51668, P51965, P60604, P61077, P61086, P61088, P62253, P62256, P62837, P63146, P68036, Q13404, Q15819, Q16763, Q5JXB2, Q5VVX9, Q712K3, Q7Z7E8, Q8N2K1, Q8WVN8, Q969T4, Q96LR5, Q9H832, Q9NPD8, Q9Y385
humans have about 40 E2s that are involved in the transfer of Ub or Ub-like (Ubl) proteins (e.g. SUMO and NEDD8). Although the majority of E2s are only twice the size of Ub, this remarkable family of enzymes performs a variety of functional roles. UBE2A functions in DNA damage repair. PCNA is monoubiquitylated by the Ube2A/B (Rad6) E2s and the RING E3 Rad18 during postreplicative DNA damage repair
physiological function
A1L167, O00762, O14933, P49427, P49459, P51668, P51965, P60604, P61077, P61086, P61088, P62253, P62256, P62837, P63146, P68036, Q13404, Q15819, Q16763, Q5JXB2, Q5VVX9, Q712K3, Q7Z7E8, Q8N2K1, Q8WVN8, Q969T4, Q96LR5, Q9H832, Q9NPD8, Q9Y385
humans have about 40 E2s that are involved in the transfer of Ub or Ub-like (Ubl) proteins (e.g. SUMO and NEDD8). Although the majority of E2s are only twice the size of Ub, this remarkable family of enzymes performs a variety of functional roles. UBE2C functions in chain-initiation of APC/C
physiological function
A1L167, O00762, O14933, P49427, P49459, P51668, P51965, P60604, P61077, P61086, P61088, P62253, P62256, P62837, P63146, P68036, Q13404, Q15819, Q16763, Q5JXB2, Q5VVX9, Q712K3, Q7Z7E8, Q8N2K1, Q8WVN8, Q969T4, Q96LR5, Q9H832, Q9NPD8, Q9Y385
humans have about 40 E2s that are involved in the transfer of Ub or Ub-like (Ubl) proteins (e.g. SUMO and NEDD8). Although the majority of E2s are only twice the size of Ub, this remarkable family of enzymes performs a variety of functional roles. UBE2G2 acts in K48 chain-building in dependence of an E3. It is an E2 involved in the ERAD pathway
physiological function
A1L167, O00762, O14933, P49427, P49459, P51668, P51965, P60604, P61077, P61086, P61088, P62253, P62256, P62837, P63146, P68036, Q13404, Q15819, Q16763, Q5JXB2, Q5VVX9, Q712K3, Q7Z7E8, Q8N2K1, Q8WVN8, Q969T4, Q96LR5, Q9H832, Q9NPD8, Q9Y385
humans have about 40 E2s that are involved in the transfer of Ub or Ub-like (Ubl) proteins (e.g. SUMO and NEDD8). Although the majority of E2s are only twice the size of Ub, this remarkable family of enzymes performs a variety of functional roles. Ube2J2 attaches Ub to the major histocompatibility complex via hydroxyl groups (serine/threonine) in collaboration with a viral RING E3 ligase. Ube2J2 ubiquitylation products are sensitive to treatment with strong base, which hydrolyzes oxyesters but not amide bonds
physiological function
A1L167, O00762, O14933, P49427, P49459, P51668, P51965, P60604, P61077, P61086, P61088, P62253, P62256, P62837, P63146, P68036, Q13404, Q15819, Q16763, Q5JXB2, Q5VVX9, Q712K3, Q7Z7E8, Q8N2K1, Q8WVN8, Q969T4, Q96LR5, Q9H832, Q9NPD8, Q9Y385
humans have about 40 E2s that are involved in the transfer of Ub or Ub-like (Ubl) proteins (e.g. SUMO and NEDD8). Although the majority of E2s are only twice the size of Ub, this remarkable family of enzymes performs a variety of functional roles. Ube2L3 plays in cell cycle regulation. Ube2L3 (UbcH7), the E2 used in many structural studies with RING-type E3s, is not reactive towards lysine and only exhibits reactivity towards cysteine. The implication is that Ube2L3, although it binds to many RING domains, is only functional as an E2 with HECT-type E3s. RBRs, such as Parkin and HHARI, have RING domains, but also contain a conserved cysteine residue that forms an obligatory E3-Ub intermediate. Thus, RBRs are functional hybrids that exploit elements found in both RING and HECT E3s
physiological function
A1L167, O00762, O14933, P49427, P49459, P51668, P51965, P60604, P61077, P61086, P61088, P62253, P62256, P62837, P63146, P68036, Q13404, Q15819, Q16763, Q5JXB2, Q5VVX9, Q712K3, Q7Z7E8, Q8N2K1, Q8WVN8, Q969T4, Q96LR5, Q9H832, Q9NPD8, Q9Y385
humans have about 40 E2s that are involved in the transfer of Ub or Ub-like (Ubl) proteins (e.g. SUMO and NEDD8). Although the majority of E2s are only twice the size of Ub, this remarkable family of enzymes performs a variety of functional roles. Ube2R1 is the cognate E2 of SCF E3 ligases
physiological function
A1L167, O00762, O14933, P49427, P49459, P51668, P51965, P60604, P61077, P61086, P61088, P62253, P62256, P62837, P63146, P68036, Q13404, Q15819, Q16763, Q5JXB2, Q5VVX9, Q712K3, Q7Z7E8, Q8N2K1, Q8WVN8, Q969T4, Q96LR5, Q9H832, Q9NPD8, Q9Y385
humans have about 40 E2s that are involved in the transfer of Ub or Ub-like (Ubl) proteins (e.g. SUMO and NEDD8). Although the majority of E2s are only twice the size of Ub, this remarkable family of enzymes performs a variety of functional roles. Ube2S is the dedicated E2 for the multi-subunit APC/C E3 that regulates cell cycle progression. On its own, Ube2S-Ub populates closed states to a considerable extent and can catalyze formation of free polyUb chains in the absence of an E3. Two non-RING subunits, Apc2 and Apc4, contribute to Ube2S activation in a mechanism that may involve the C-terminal helix of the Ube2S UBC domain
physiological function
A1L167, O00762, O14933, P49427, P49459, P51668, P51965, P60604, P61077, P61086, P61088, P62253, P62256, P62837, P63146, P68036, Q13404, Q15819, Q16763, Q5JXB2, Q5VVX9, Q712K3, Q7Z7E8, Q8N2K1, Q8WVN8, Q969T4, Q96LR5, Q9H832, Q9NPD8, Q9Y385
humans have about 40 E2s that are involved in the transfer of Ub or Ub-like (Ubl) proteins (e.g. SUMO and NEDD8). Although the majority of E2s are only twice the size of Ub, this remarkable family of enzymes performs a variety of functional roles. Ube2T, the E2 involved in the Fanconi Anemia DNA repair pathway and specific for E3 ligase FANCL, transfers Ub to a lysine near its active site and two lysines located in its C-terminal extension. Ubiquitylated Ube2T has been observed in vitro and in cells, and its production is enhanced by the E3, FANCL. Unlike Ubc7 autoubiquitylation, (multi)-monoubiquitylated Ube2T does not signal for its degradation, but has decreased Ub transfer activity in vitro
physiological function
A1L167, O00762, O14933, P49427, P49459, P51668, P51965, P60604, P61077, P61086, P61088, P62253, P62256, P62837, P63146, P68036, Q13404, Q15819, Q16763, Q5JXB2, Q5VVX9, Q712K3, Q7Z7E8, Q8N2K1, Q8WVN8, Q969T4, Q96LR5, Q9H832, Q9NPD8, Q9Y385
humans have about 40 E2s that are involved in the transfer of Ub or Ub-like (Ubl) proteins (e.g. SUMO and NEDD8). Although the majority of E2s are only twice the size of Ub, this remarkable family of enzymes performs a variety of functional roles. Ube2W (EC 2.3.2.25) can serve as the template for chain building by Ube2N and Ube2K
physiological function
A1L167, O00762, O14933, P49427, P49459, P51668, P51965, P60604, P61077, P61086, P61088, P62253, P62256, P62837, P63146, P68036, Q13404, Q15819, Q16763, Q5JXB2, Q5VVX9, Q712K3, Q7Z7E8, Q8N2K1, Q8WVN8, Q969T4, Q96LR5, Q9H832, Q9NPD8, Q9Y385
humans have about 40 E2s that are involved in the transfer of Ub or Ub-like (Ubl) proteins (e.g., SUMO and NEDD8). Although the majority of E2s are only twice the size of Ub, this remarkable family of enzymes performs a variety of functional roles. Enzyme Ube2D2 is a promiscuous lysine- and cysteine-reactive E2. OTUB1 DUB activity is enhanced by interaction with free E2s. Binding of Ube2D2 stabilizes the disordered OTUB1 N-terminus in an alpha-helical conformation, which completes the binding site for K48-linked diUb. The E2-mediated conformational change decreases the Km of OTUB1 for diUb by over 35fold, thereby enhancing the rate of OTUB1-dependent polyUb degradation. The E2 acting as an effector protein to stimulate enzyme (DUB) activity
physiological function
A1L167, O00762, O14933, P49427, P49459, P51668, P51965, P60604, P61077, P61086, P61088, P62253, P62256, P62837, P63146, P68036, Q13404, Q15819, Q16763, Q5JXB2, Q5VVX9, Q712K3, Q7Z7E8, Q8N2K1, Q8WVN8, Q969T4, Q96LR5, Q9H832, Q9NPD8, Q9Y385
humans have about 40 E2s that are involved in the transfer of Ub or Ub-like (Ubl) proteins (e.g., SUMO and NEDD8). Although the majority of E2s are only twice the size of Ub, this remarkable family of enzymes performs a variety of functional roles. UBE2B functions in DNA damage repair. The chain-building activity of other E2s is enhanced by Ub backside binding as well. The interaction is critical for the E3-independent ability of Ube2B to build K11-linked polyUb chains. PCNA is monoubiquitylated by the Ube2A/B (Rad6) E2s and the RING E3 Rad18 during postreplicative DNA damage repair
physiological function
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involvement of ubiquitin-conjugating enzyme (UBC) in ripening process and response to cold and heat stress of Vitis vinifera
physiological function
MARCH6, an E3 ubiquitin ligase, specifically promotes cholesterol-stimulated ubiquitylation and subsequent proteasomal degradation of squalene monooxygenase (SQLE), but not of 3-hydroxy-3-methylglutaryl coenzyme A reductase (HMGCR). The sterol-dependent degradation machinery makes use of distinct E2 ubiquitin conjugating enzymes
physiological function
the E2 ubiquitin-conjugating enzyme UBE2G2 is broadly involved in regulating the downregulation of immunoreceptors targeted by HCMV US2. The E2 ubiquitin conjugating enzyme UBE2G2 to be essential for US2-mediated HLA-I downregulation
physiological function
the E2 ubiquitin-conjugating enzyme UBE2J2 is broadly involved in regulating the downregulation of immunoreceptors targeted by HCMV US2
physiological function
UBC6e is an E2 ubiquitin conjugating enzyme that localizes to the ER via its tail-anchor. Functional UBC6e requires its precise location in the endoplasmic reticulum (ER) to form a supramolecular complex with Derlin2. This complex targets ERAD enhancers for degradation, a function that depends on UBC6e's enzymatic activity. UBC6e-/- cells upregulate ERAD enhancers selectively, but UBC6e downregulates EDEM1, EDEM3, OS-9 and SEL1L (ERAD enhancers) in the absence of ER stress. Homeostasis of SEL1L, EDEM1 and OS-9 requires enzymatic activity of UBC6e. UBC6e's function depends strictly on its E2 enzymatic activity but not its phosphorylation status. The exact ER membrane localization of UBC6e and the supramolecular complexes in which UBC6e participates determine its activity, and directly control the levels of components essential for ERAD activity. Only the Derlin2-complexed UBC6e controls the levels of ERAD enhancers
physiological function
UBE2J2 is a new regulator of cellular cholesterol homeostasis in mammalian cells. MARCH6, an E3 ubiquitin ligase, specifically promotes cholesterol-stimulated ubiquitylation and subsequent proteasomal degradation of squalene monooxygenase (SQLE), but not of 3-hydroxy-3-methylglutaryl coenzyme A reductase (HMGCR). The sterol-dependent degradation machinery makes use of distinct E2 ubiquitin conjugating enzymes. The ability of UBE2J2 to support SQLE degradation critically depends on its enzymatic activity. UBE2J2 as an important partner of MARCH6 in cholesterol-stimulated degradation of SQLE, thereby contributing to the complex regulation of cellular cholesterol homeostasis
physiological function
Ube2T is the E2 ubiquitin-conjugating enzyme of the Fanconi anemia DNA repair pathway. Together with FANCL (the E3 ligase), Ube2T catalyzes the monoubiquitination of the heterodimeric FANCI/FANCD2 complex, which is the key signaling event to activate the FA pathway for DNA repair
physiological function
UBE2Z is a selective E2 enzyme, functioning in ubiquitination only with E1-like ubiquitin-activating enzyme UBA6
physiological function
ubiquitin (Ub) signaling requires the sequential interactions and activities of three enzymes, E1, E2, and E3. Cdc34 is an E2 that plays a key role in regulating cell cycle progression and requires unique structural elements to function, molecular mechanisms by which Cdc34 function in cells, overview
physiological function
ubiquitin (Ub) signaling requires the sequential interactions and activities of three enzymes, E1, E2, and E3. Cdc34 is an E2 that plays a key role in regulating cell cycle progression and requires unique structural elements to function, molecular mechanisms by which Cdc34 function in cells, overview. An ordered Cdc34 CTDprox extension is involved in Ub discharge, CTDprox/Ub contacts are important for Cdc34 action in cells. Cdc34 CTDprox locks Ub(t) in the closed conformation. The Cdc34 CTDprox extension is involved in Ub discharge
physiological function
ubiquitin signalling is a fundamental eukaryotic regulatory system, controlling diverse cellular functions. A cascade of E1, E2, and E3 enzymes is required for assembly of distinct signals, whereas an array of deubiquitinases and ubiquitin-binding modules edit, remove, and translate the signals. In the centre of this cascade sits the E2-conjugating enzyme, relaying activated ubiquitin from the E1 activating enzyme to the substrate, usually via an E3 ubiquitin ligase. Function of UBE2L3 with HOIL-1L-interacting protein (HOIP) in cancer. HOIL-1L is the haem-oxidized IRP2 ubiquitin ligase-1. Functional association of UBE2L3 with Parkinson's disease (PD). Parkin E3 ligase activity is auto-inhibited by the N-terminal UBL domain, which obscures the catalytic interaction between Parkin and the ubiquitin-loaded E2. Parkin apparently employs different E2 enzymes to generate distinct ubiquitin chain signals that mediate efficient mitophagy. The apparent redundant functions of UBE2L3 with other E2s may explain the current lack of any genetic association of UBE2L3 gene alterations with PD
physiological function
ubiquitin signalling is a fundamental eukaryotic regulatory system, controlling diverse cellular functions. A cascade of E1, E2, and E3 enzymes is required for assembly of distinct signals, whereas an array of deubiquitinases and ubiquitin-binding modules edit, remove, and translate the signals. In the centre of this cascade sits the E2-conjugating enzyme, relaying activated ubiquitin from the E1 activating enzyme to the substrate, usually via an E3 ubiquitin ligase. UBE2T has potential oncogenic and tumour suppressor function in carcinogenesis
physiological function
ubiquitin-conjugating enzyme E2 B (UBE2B) is a regulator of O6-methylguanine-DNA methyltransferase (MGMT) ubiquitination mediated by 1,3-bis(2-chloroethyl)-1-nitrosourea (BCNU)in nasopharyngeal carcinoma (NPC) cells. BCNU enhances the interaction between MGMT, RAD18, and ubiquitinated UBE2B. The E3 ubiquitin ligase RAD18, a partner of UBE2B, is also involved in BCNU-mediated MGMT ubiquitination. UBE2B modulates sensitivity to BCNU in NPC cells by regulating MGMT ubiquitination. UBE2B and RAD18 facilitate and accelerate MGMT ubiquitination in vitro, and BCNU and O6-benzylguanine promote UBE2B/RAD18-induced MGMT ubiquitination
physiological function
ubiquitin-conjugating enzyme E2 D1 (Ube2D1) mediates lysine-independent ubiquitination of the E3 ubiquitin ligase March-I, which contributes to March-I turnover. March-I is a membrane-bound E3 ubiquitin ligase belonging to the membrane-associated RING-CH (March) family. March-I ubiquitinates and downregulates the expression of major histocompatibility complex (MHC) class II and cluster of differentiation 86 (CD86) in antigen-presenting cells. Molecular mechanism regulating March-I ubiquitination, overview. March-I is not ubiquinated on a lysine residue. March-I E3 ligase activity is not required for its ubiquitination and does not regulate March-I protein expression. March-I does not undergo autoubiquitination. Ube2D1 together with another E3 ubiquitin ligase regulates March-I expression. March-I is oligo-ubiquitinated and undergoes proteolytic degradation
physiological function
ubiquitination process consists of three main steps: the first step is activation: ubiquitin is activated by an E1 ubiquitin-activating enzyme, which is dependent on ATP. The second step is conjugation: E2 ubiquitin-conjugating enzymes catalyze the transfer of ubiquitin from E1 to the active site cysteine of the E2 via a trans(thio)esterification reaction. The third step is ligation: E3 ubiquitin ligases catalyze the final step of the ubiquitination cascade. Most commonly, they create an isopeptide bond between a lysine of the target protein and the C-terminal glycine of ubiquitin. E2 ubiquitin-conjugating enzymes RAD6A and RAD6B are interacting with E3 ubiquitin ligase RNF168 and RAD18 in response to DNA damage, recombinant coexpression and interaction analysis, overview. Following the localization of E3 enzymes to DNA damage sites, the E2 enzymes are recruited to these sites, where they catalyze protein ubiquitination. DNA damage-induced foci of E2 ubiquitin-conjugating enzyme require E3 ubiquitin ligase for its formation in mammalian cells. RNF168 or RAD18 recruit RAD6A and RAD6B to DNA damage sites, the interaction is specific, no other E3 ligases intecat with Rad6A/Rad6B
physiological function
ubiquitination process consists of three main steps: the first step is activation: ubiquitin is activated by an E1 ubiquitin-activating enzyme, which is dependent on ATP. The second step is conjugation: E2 ubiquitin-conjugating enzymes catalyze the transfer of ubiquitin from E1 to the active site cysteine of the E2 via a trans(thio)esterification reaction. The third step is ligation: E3 ubiquitin ligases catalyze the final step of the ubiquitination cascade. Most commonly, they create an isopeptide bond between a lysine of the target protein and the C-terminal glycine of ubiquitin. E2 ubiquitin-conjugating enzymes RAD6A and RAD6B are interacting with E3 ubiquitin ligase RNF168 and RAD18 in response to DNA damage, recombinant coexpression and interaction analysis, overview. Following the localization of E3 enzymes to DNA damage sites, the E2 enzymes are recruited to these sites, where they catalyze protein ubiquitination. DNA damage-induced foci of E2 ubiquitin-conjugating enzyme require E3 ubiquitin ligase for its formation in mammalian cells. RNF168 or RAD18 recruit RAD6A and RAD6B to DNA damage sites, the interaction is specific, no other E3 ligases interact with Rad6A/Rad6B
physiological function
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the enzyme is critical for tombvirus replication and is involved in promoting the subversion of Vps23p and Vps4p ESCRT proteins for viral replicase complex assembly
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physiological function
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the enzyme is correlated with the cryogenic autolysis of Volvariella volvacea
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physiological function
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Ubc11 gene encodes one of the two E2 enzymes required for progression through mitosis in fission yeast
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physiological function
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ubiquitin (Ub) signaling requires the sequential interactions and activities of three enzymes, E1, E2, and E3. Cdc34 is an E2 that plays a key role in regulating cell cycle progression and requires unique structural elements to function, molecular mechanisms by which Cdc34 function in cells, overview. An ordered Cdc34 CTDprox extension is involved in Ub discharge, CTDprox/Ub contacts are important for Cdc34 action in cells. Cdc34 CTDprox locks Ub(t) in the closed conformation. The Cdc34 CTDprox extension is involved in Ub discharge
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additional information
active site gate dynamics modulate the catalytic activity of the ubiquitination enzyme E2-25K. NMR study of purified recombinant detagged wild-type and mutant enzymes, analysis of enzyme structure and E2-25K-ubiquitin interaction, overview. Molecular dynamics simulations for E2-25K and the Q126L/D127G active site gate mutants
additional information
analyis of the molecular basis by which Cdc34 engages its E1, and the structural mechanisms, by which its unique C-terminal extension functions in Cdc34 activity. Conformational changes in Uba1 and Cdc34 and a unique binding mode are required for transthiolation. The Cdc34-Ub structure reveals contacts between the Cdc34 C-terminal extension and Ub that stabilize Cdc34-Ub in a closed conformation and are critical for Ub discharge
additional information
analyis of the molecular basis by which Cdc34 engages its E1, and the structural mechanisms, by which its unique C-terminal extension functions in Cdc34 activity. Conformational changes in Uba1 and Cdc34 and a unique binding mode are required for transthiolation. The Cdc34-Ub structure reveals contacts between the Cdc34 C-terminal extension and Ub that stabilize Cdc34-Ub in a closed conformation and are critical for Ub discharge
additional information
construction of initial Ube2R1-Rbx1 models, Rbx1 (PDB ID 2LGV) and Ube2R1 (PDB ID 4MDK) are aligned to the respective components from the Ube2G2/Rnf45 cocrystal structure (PDB ID 2LXP) and energy is minimized with Rosetta algorithms relax and fixbb. Next, an initial conformation for the acidic loop (residues 97 to 115) is built onto the top-scoring Ube2R1-Rbx1 model using the CCD algorithm with fragments derived from the Ube2R1 amino acid sequence. This model of the Ube2R1-Rbx1 complex is used to create initial models of the Ube2R1-donor ubiquitin/acceptor ubiquitin-Rbx1 complex using the UBQ_E2_thioester protocol, which allows the user to sequentially model the orientation of the thioesterified donor ubiquitin and the approach of an acceptor ubiquitin and to perform standard loop modeling on the acidic loop. The acceptor ubiquitin is based on an apo structure (PDB ID 1UBQ). To generate models consistent with the crystallized orientation of donor ubiquitin, a constraint was implemented between Leu129 on Ube2R1 and both Ile44 and Val70 on the donor ubiquitin. Using this procedure, 4000 theoretical models of Ube2R1-donor ubiquitin/acceptor ubiquitin-Rbx1 are generated yielding 286 low-scoring models. Refining the acceptor ubiquitin and acidic loop. Ube2R1 structural modeling, overview. Molecular modeling of the Ube2R1-donor ubiquitin/acceptor ubiquitin-Rbx1 complex results in 14 distinct clusters of the Ube2R1-acceptor ubiquitin conformation
additional information
construction of initial Ube2R1-Rbx1 models, Rbx1 (PDB ID 2LGV) and Ube2R1 (PDB ID 4MDK) are aligned to the respective components from the Ube2G2/Rnf45 cocrystal structure (PDB ID 2LXP) and energy is minimized with Rosetta algorithms relax and fixbb. Next, an initial conformation for the acidic loop (residues 97 to 115) is built onto the top-scoring Ube2R1-Rbx1 model using the CCD algorithm with fragments derived from the Ube2R1 amino acid sequence. This model of the Ube2R1-Rbx1 complex is used to create initial models of the Ube2R1-donor ubiquitin/acceptor ubiquitin-Rbx1 complex using the UBQ_E2_thioester protocol, which allows the user to sequentially model the orientation of the thioesterified donor ubiquitin and the approach of an acceptor ubiquitin and to perform standard loop modeling on the acidic loop. The acceptor ubiquitin is based on an apo structure (PDB ID 1UBQ). To generate models consistent with the crystallized orientation of donor ubiquitin, a constraint was implemented between Leu129 on Ube2R1 and both Ile44 and Val70 on the donor ubiquitin. Using this procedure, 4000 theoretical models of Ube2R1-donor ubiquitin/acceptor ubiquitin-Rbx1 are generated yielding 286 low-scoring models. Refining the acceptor ubiquitin and acidic loop. Ube2R1 structural modeling, overview. Molecular modeling of the Ube2R1-donor ubiquitin/acceptor ubiquitin-Rbx1 complex results in 14 distinct clusters of the Ube2R1-acceptor ubiquitin conformation
additional information
E2 structure-function analysis, overview. Deletion of the N-terminal extension of Ube2E family members switches their (in vitro) activity from mono- to polyubiquitylation
additional information
E2 structure-function analysis, overview. Deletion of the N-terminal extension of Ube2E family members switches their (in vitro) activity from mono- to polyubiquitylation
additional information
E2 structure-function analysis, overview. Deletion of the N-terminal extension of Ube2E family members switches their (in vitro) activity from mono- to polyubiquitylation
additional information
E2 structure-function analysis, overview. Deletion of the N-terminal extension of Ube2E family members switches their (in vitro) activity from mono- to polyubiquitylation
additional information
E2 structure-function analysis, overview. Deletion of the N-terminal extension of Ube2E family members switches their (in vitro) activity from mono- to polyubiquitylation
additional information
E2 structure-function analysis, overview. Deletion of the N-terminal extension of Ube2E family members switches their (in vitro) activity from mono- to polyubiquitylation
additional information
E2 structure-function analysis, overview. Deletion of the N-terminal extension of Ube2E family members switches their (in vitro) activity from mono- to polyubiquitylation
additional information
E2 structure-function analysis, overview. Deletion of the N-terminal extension of Ube2E family members switches their (in vitro) activity from mono- to polyubiquitylation
additional information
E2 structure-function analysis, overview. Deletion of the N-terminal extension of Ube2E family members switches their (in vitro) activity from mono- to polyubiquitylation
additional information
E2 structure-function analysis, overview. Deletion of the N-terminal extension of Ube2E family members switches their (in vitro) activity from mono- to polyubiquitylation
additional information
E2 structure-function analysis, overview. Deletion of the N-terminal extension of Ube2E family members switches their (in vitro) activity from mono- to polyubiquitylation
additional information
E2 structure-function analysis, overview. Deletion of the N-terminal extension of Ube2E family members switches their (in vitro) activity from mono- to polyubiquitylation
additional information
E2 structure-function analysis, overview. Deletion of the N-terminal extension of Ube2E family members switches their (in vitro) activity from mono- to polyubiquitylation
additional information
E2 structure-function analysis, overview. Deletion of the N-terminal extension of Ube2E family members switches their (in vitro) activity from mono- to polyubiquitylation
additional information
E2 structure-function analysis, overview. Deletion of the N-terminal extension of Ube2E family members switches their (in vitro) activity from mono- to polyubiquitylation
additional information
E2 structure-function analysis, overview. Deletion of the N-terminal extension of Ube2E family members switches their (in vitro) activity from mono- to polyubiquitylation
additional information
E2 structure-function analysis, overview. Deletion of the N-terminal extension of Ube2E family members switches their (in vitro) activity from mono- to polyubiquitylation
additional information
E2 structure-function analysis, overview. Deletion of the N-terminal extension of Ube2E family members switches their (in vitro) activity from mono- to polyubiquitylation
additional information
E2 structure-function analysis, overview. Deletion of the N-terminal extension of Ube2E family members switches their (in vitro) activity from mono- to polyubiquitylation
additional information
E2 structure-function analysis, overview. Deletion of the N-terminal extension of Ube2E family members switches their (in vitro) activity from mono- to polyubiquitylation
additional information
E2 structure-function analysis, overview. Deletion of the N-terminal extension of Ube2E family members switches their (in vitro) activity from mono- to polyubiquitylation
additional information
E2 structure-function analysis, overview. Deletion of the N-terminal extension of Ube2E family members switches their (in vitro) activity from mono- to polyubiquitylation
additional information
E2 structure-function analysis, overview. Deletion of the N-terminal extension of Ube2E family members switches their (in vitro) activity from mono- to polyubiquitylation
additional information
E2 structure-function analysis, overview. Deletion of the N-terminal extension of Ube2E family members switches their (in vitro) activity from mono- to polyubiquitylation
additional information
E2 structure-function analysis, overview. Deletion of the N-terminal extension of Ube2E family members switches their (in vitro) activity from mono- to polyubiquitylation
additional information
E2 structure-function analysis, overview. Deletion of the N-terminal extension of Ube2E family members switches their (in vitro) activity from mono- to polyubiquitylation
additional information
E2 structure-function analysis, overview. Deletion of the N-terminal extension of Ube2E family members switches their (in vitro) activity from mono- to polyubiquitylation
additional information
E2 structure-function analysis, overview. Deletion of the N-terminal extension of Ube2E family members switches their (in vitro) activity from mono- to polyubiquitylation
additional information
E2 structure-function analysis, overview. Deletion of the N-terminal extension of Ube2E family members switches their (in vitro) activity from mono- to polyubiquitylation
additional information
E2 structure-function analysis, overview. Deletion of the N-terminal extension of Ube2E family members switches their (in vitro) activity from mono- to polyubiquitylation
additional information
E2 structure-function analysis, overview. Enzyme UBE2NL has no catalytic cysteine
additional information
E2 structure-function analysis, overview. Enzyme UBE2NL has no catalytic cysteine
additional information
E2 structure-function analysis, overview. Enzyme UBE2NL has no catalytic cysteine
additional information
E2 structure-function analysis, overview. Enzyme UBE2NL has no catalytic cysteine
additional information
E2 structure-function analysis, overview. Enzyme UBE2NL has no catalytic cysteine
additional information
E2 structure-function analysis, overview. Enzyme UBE2NL has no catalytic cysteine
additional information
E2 structure-function analysis, overview. Enzyme UBE2NL has no catalytic cysteine
additional information
E2 structure-function analysis, overview. Enzyme UBE2NL has no catalytic cysteine
additional information
E2 structure-function analysis, overview. Enzyme UBE2NL has no catalytic cysteine
additional information
E2 structure-function analysis, overview. Enzyme UBE2NL has no catalytic cysteine
additional information
E2 structure-function analysis, overview. Enzyme UBE2NL has no catalytic cysteine
additional information
E2 structure-function analysis, overview. Enzyme UBE2NL has no catalytic cysteine
additional information
E2 structure-function analysis, overview. Enzyme UBE2NL has no catalytic cysteine
additional information
E2 structure-function analysis, overview. Enzyme UBE2NL has no catalytic cysteine
additional information
E2 structure-function analysis, overview. Enzyme UBE2NL has no catalytic cysteine
additional information
E2 structure-function analysis, overview. Enzyme UBE2NL has no catalytic cysteine
additional information
E2 structure-function analysis, overview. Enzyme UBE2NL has no catalytic cysteine
additional information
E2 structure-function analysis, overview. Enzyme UBE2NL has no catalytic cysteine
additional information
E2 structure-function analysis, overview. Enzyme UBE2NL has no catalytic cysteine
additional information
E2 structure-function analysis, overview. Enzyme UBE2NL has no catalytic cysteine
additional information
E2 structure-function analysis, overview. Enzyme UBE2NL has no catalytic cysteine
additional information
E2 structure-function analysis, overview. Enzyme UBE2NL has no catalytic cysteine
additional information
E2 structure-function analysis, overview. Enzyme UBE2NL has no catalytic cysteine
additional information
E2 structure-function analysis, overview. Enzyme UBE2NL has no catalytic cysteine
additional information
E2 structure-function analysis, overview. Enzyme UBE2NL has no catalytic cysteine
additional information
E2 structure-function analysis, overview. Enzyme UBE2NL has no catalytic cysteine
additional information
E2 structure-function analysis, overview. Enzyme UBE2NL has no catalytic cysteine
additional information
E2 structure-function analysis, overview. Enzyme UBE2NL has no catalytic cysteine
additional information
E2 structure-function analysis, overview. Enzyme UBE2NL has no catalytic cysteine
additional information
E2 structure-function analysis, overview. Enzyme UBE2NL has no catalytic cysteine
additional information
E2 structure-function analysis, overview. K48-specific Ube2R1 has a short about 12 amino acid insertion proximal to the E2 active site that determines specificity
additional information
E2 structure-function analysis, overview. K48-specific Ube2R1 has a short about 12 amino acid insertion proximal to the E2 active site that determines specificity
additional information
E2 structure-function analysis, overview. K48-specific Ube2R1 has a short about 12 amino acid insertion proximal to the E2 active site that determines specificity
additional information
E2 structure-function analysis, overview. K48-specific Ube2R1 has a short about 12 amino acid insertion proximal to the E2 active site that determines specificity
additional information
E2 structure-function analysis, overview. K48-specific Ube2R1 has a short about 12 amino acid insertion proximal to the E2 active site that determines specificity
additional information
E2 structure-function analysis, overview. K48-specific Ube2R1 has a short about 12 amino acid insertion proximal to the E2 active site that determines specificity
additional information
E2 structure-function analysis, overview. K48-specific Ube2R1 has a short about 12 amino acid insertion proximal to the E2 active site that determines specificity
additional information
E2 structure-function analysis, overview. K48-specific Ube2R1 has a short about 12 amino acid insertion proximal to the E2 active site that determines specificity
additional information
E2 structure-function analysis, overview. K48-specific Ube2R1 has a short about 12 amino acid insertion proximal to the E2 active site that determines specificity
additional information
E2 structure-function analysis, overview. K48-specific Ube2R1 has a short about 12 amino acid insertion proximal to the E2 active site that determines specificity
additional information
E2 structure-function analysis, overview. K48-specific Ube2R1 has a short about 12 amino acid insertion proximal to the E2 active site that determines specificity
additional information
E2 structure-function analysis, overview. K48-specific Ube2R1 has a short about 12 amino acid insertion proximal to the E2 active site that determines specificity
additional information
E2 structure-function analysis, overview. K48-specific Ube2R1 has a short about 12 amino acid insertion proximal to the E2 active site that determines specificity
additional information
E2 structure-function analysis, overview. K48-specific Ube2R1 has a short about 12 amino acid insertion proximal to the E2 active site that determines specificity
additional information
E2 structure-function analysis, overview. K48-specific Ube2R1 has a short about 12 amino acid insertion proximal to the E2 active site that determines specificity
additional information
E2 structure-function analysis, overview. K48-specific Ube2R1 has a short about 12 amino acid insertion proximal to the E2 active site that determines specificity
additional information
E2 structure-function analysis, overview. K48-specific Ube2R1 has a short about 12 amino acid insertion proximal to the E2 active site that determines specificity
additional information
E2 structure-function analysis, overview. K48-specific Ube2R1 has a short about 12 amino acid insertion proximal to the E2 active site that determines specificity
additional information
E2 structure-function analysis, overview. K48-specific Ube2R1 has a short about 12 amino acid insertion proximal to the E2 active site that determines specificity
additional information
E2 structure-function analysis, overview. K48-specific Ube2R1 has a short about 12 amino acid insertion proximal to the E2 active site that determines specificity
additional information
E2 structure-function analysis, overview. K48-specific Ube2R1 has a short about 12 amino acid insertion proximal to the E2 active site that determines specificity
additional information
E2 structure-function analysis, overview. K48-specific Ube2R1 has a short about 12 amino acid insertion proximal to the E2 active site that determines specificity
additional information
E2 structure-function analysis, overview. K48-specific Ube2R1 has a short about 12 amino acid insertion proximal to the E2 active site that determines specificity
additional information
E2 structure-function analysis, overview. K48-specific Ube2R1 has a short about 12 amino acid insertion proximal to the E2 active site that determines specificity
additional information
E2 structure-function analysis, overview. K48-specific Ube2R1 has a short about 12 amino acid insertion proximal to the E2 active site that determines specificity
additional information
E2 structure-function analysis, overview. K48-specific Ube2R1 has a short about 12 amino acid insertion proximal to the E2 active site that determines specificity
additional information
E2 structure-function analysis, overview. K48-specific Ube2R1 has a short about 12 amino acid insertion proximal to the E2 active site that determines specificity
additional information
E2 structure-function analysis, overview. K48-specific Ube2R1 has a short about 12 amino acid insertion proximal to the E2 active site that determines specificity
additional information
E2 structure-function analysis, overview. K48-specific Ube2R1 has a short about 12 amino acid insertion proximal to the E2 active site that determines specificity
additional information
E2 structure-function analysis, overview. K48-specific Ube2R1 has a short about 12 amino acid insertion proximal to the E2 active site that determines specificity
additional information
E2 structure-function analysis, overview. K48-specific Ube2R2 has a short about 12 amino acid insertion proximal to the E2 active site that determines specificity
additional information
E2 structure-function analysis, overview. K48-specific Ube2R2 has a short about 12 amino acid insertion proximal to the E2 active site that determines specificity
additional information
E2 structure-function analysis, overview. K48-specific Ube2R2 has a short about 12 amino acid insertion proximal to the E2 active site that determines specificity
additional information
E2 structure-function analysis, overview. K48-specific Ube2R2 has a short about 12 amino acid insertion proximal to the E2 active site that determines specificity
additional information
E2 structure-function analysis, overview. K48-specific Ube2R2 has a short about 12 amino acid insertion proximal to the E2 active site that determines specificity
additional information
E2 structure-function analysis, overview. K48-specific Ube2R2 has a short about 12 amino acid insertion proximal to the E2 active site that determines specificity
additional information
E2 structure-function analysis, overview. K48-specific Ube2R2 has a short about 12 amino acid insertion proximal to the E2 active site that determines specificity
additional information
E2 structure-function analysis, overview. K48-specific Ube2R2 has a short about 12 amino acid insertion proximal to the E2 active site that determines specificity
additional information
E2 structure-function analysis, overview. K48-specific Ube2R2 has a short about 12 amino acid insertion proximal to the E2 active site that determines specificity
additional information
E2 structure-function analysis, overview. K48-specific Ube2R2 has a short about 12 amino acid insertion proximal to the E2 active site that determines specificity
additional information
E2 structure-function analysis, overview. K48-specific Ube2R2 has a short about 12 amino acid insertion proximal to the E2 active site that determines specificity
additional information
E2 structure-function analysis, overview. K48-specific Ube2R2 has a short about 12 amino acid insertion proximal to the E2 active site that determines specificity
additional information
E2 structure-function analysis, overview. K48-specific Ube2R2 has a short about 12 amino acid insertion proximal to the E2 active site that determines specificity
additional information
E2 structure-function analysis, overview. K48-specific Ube2R2 has a short about 12 amino acid insertion proximal to the E2 active site that determines specificity
additional information
E2 structure-function analysis, overview. K48-specific Ube2R2 has a short about 12 amino acid insertion proximal to the E2 active site that determines specificity
additional information
E2 structure-function analysis, overview. K48-specific Ube2R2 has a short about 12 amino acid insertion proximal to the E2 active site that determines specificity
additional information
E2 structure-function analysis, overview. K48-specific Ube2R2 has a short about 12 amino acid insertion proximal to the E2 active site that determines specificity
additional information
E2 structure-function analysis, overview. K48-specific Ube2R2 has a short about 12 amino acid insertion proximal to the E2 active site that determines specificity
additional information
E2 structure-function analysis, overview. K48-specific Ube2R2 has a short about 12 amino acid insertion proximal to the E2 active site that determines specificity
additional information
E2 structure-function analysis, overview. K48-specific Ube2R2 has a short about 12 amino acid insertion proximal to the E2 active site that determines specificity
additional information
E2 structure-function analysis, overview. K48-specific Ube2R2 has a short about 12 amino acid insertion proximal to the E2 active site that determines specificity
additional information
E2 structure-function analysis, overview. K48-specific Ube2R2 has a short about 12 amino acid insertion proximal to the E2 active site that determines specificity
additional information
E2 structure-function analysis, overview. K48-specific Ube2R2 has a short about 12 amino acid insertion proximal to the E2 active site that determines specificity
additional information
E2 structure-function analysis, overview. K48-specific Ube2R2 has a short about 12 amino acid insertion proximal to the E2 active site that determines specificity
additional information
E2 structure-function analysis, overview. K48-specific Ube2R2 has a short about 12 amino acid insertion proximal to the E2 active site that determines specificity
additional information
E2 structure-function analysis, overview. K48-specific Ube2R2 has a short about 12 amino acid insertion proximal to the E2 active site that determines specificity
additional information
E2 structure-function analysis, overview. K48-specific Ube2R2 has a short about 12 amino acid insertion proximal to the E2 active site that determines specificity
additional information
E2 structure-function analysis, overview. K48-specific Ube2R2 has a short about 12 amino acid insertion proximal to the E2 active site that determines specificity
additional information
E2 structure-function analysis, overview. K48-specific Ube2R2 has a short about 12 amino acid insertion proximal to the E2 active site that determines specificity
additional information
E2 structure-function analysis, overview. K48-specific Ube2R2 has a short about 12 amino acid insertion proximal to the E2 active site that determines specificity
additional information
E2 structure-function analysis, overview. Multi-subunit E3s make use of the E2 backside surface. The APC/C engages Ube2C using both a RING subunit Apc11 and the WHB domain of a cullin subunit Apc2, the latter interaction being via the E2's backside. While use of two subunits to recruit the E2 serves to ensure specificity for Ube2C, the additional interaction also appears to direct substrate ubiquitylation by reducing the degrees of freedom available for the E2/RING assembly
additional information
E2 structure-function analysis, overview. Multi-subunit E3s make use of the E2 backside surface. The APC/C engages Ube2C using both a RING subunit Apc11 and the WHB domain of a cullin subunit Apc2, the latter interaction being via the E2's backside. While use of two subunits to recruit the E2 serves to ensure specificity for Ube2C, the additional interaction also appears to direct substrate ubiquitylation by reducing the degrees of freedom available for the E2/RING assembly
additional information
E2 structure-function analysis, overview. Multi-subunit E3s make use of the E2 backside surface. The APC/C engages Ube2C using both a RING subunit Apc11 and the WHB domain of a cullin subunit Apc2, the latter interaction being via the E2's backside. While use of two subunits to recruit the E2 serves to ensure specificity for Ube2C, the additional interaction also appears to direct substrate ubiquitylation by reducing the degrees of freedom available for the E2/RING assembly
additional information
E2 structure-function analysis, overview. Multi-subunit E3s make use of the E2 backside surface. The APC/C engages Ube2C using both a RING subunit Apc11 and the WHB domain of a cullin subunit Apc2, the latter interaction being via the E2's backside. While use of two subunits to recruit the E2 serves to ensure specificity for Ube2C, the additional interaction also appears to direct substrate ubiquitylation by reducing the degrees of freedom available for the E2/RING assembly
additional information
E2 structure-function analysis, overview. Multi-subunit E3s make use of the E2 backside surface. The APC/C engages Ube2C using both a RING subunit Apc11 and the WHB domain of a cullin subunit Apc2, the latter interaction being via the E2's backside. While use of two subunits to recruit the E2 serves to ensure specificity for Ube2C, the additional interaction also appears to direct substrate ubiquitylation by reducing the degrees of freedom available for the E2/RING assembly
additional information
E2 structure-function analysis, overview. Multi-subunit E3s make use of the E2 backside surface. The APC/C engages Ube2C using both a RING subunit Apc11 and the WHB domain of a cullin subunit Apc2, the latter interaction being via the E2's backside. While use of two subunits to recruit the E2 serves to ensure specificity for Ube2C, the additional interaction also appears to direct substrate ubiquitylation by reducing the degrees of freedom available for the E2/RING assembly
additional information
E2 structure-function analysis, overview. Multi-subunit E3s make use of the E2 backside surface. The APC/C engages Ube2C using both a RING subunit Apc11 and the WHB domain of a cullin subunit Apc2, the latter interaction being via the E2's backside. While use of two subunits to recruit the E2 serves to ensure specificity for Ube2C, the additional interaction also appears to direct substrate ubiquitylation by reducing the degrees of freedom available for the E2/RING assembly
additional information
E2 structure-function analysis, overview. Multi-subunit E3s make use of the E2 backside surface. The APC/C engages Ube2C using both a RING subunit Apc11 and the WHB domain of a cullin subunit Apc2, the latter interaction being via the E2's backside. While use of two subunits to recruit the E2 serves to ensure specificity for Ube2C, the additional interaction also appears to direct substrate ubiquitylation by reducing the degrees of freedom available for the E2/RING assembly
additional information
E2 structure-function analysis, overview. Multi-subunit E3s make use of the E2 backside surface. The APC/C engages Ube2C using both a RING subunit Apc11 and the WHB domain of a cullin subunit Apc2, the latter interaction being via the E2's backside. While use of two subunits to recruit the E2 serves to ensure specificity for Ube2C, the additional interaction also appears to direct substrate ubiquitylation by reducing the degrees of freedom available for the E2/RING assembly
additional information
E2 structure-function analysis, overview. Multi-subunit E3s make use of the E2 backside surface. The APC/C engages Ube2C using both a RING subunit Apc11 and the WHB domain of a cullin subunit Apc2, the latter interaction being via the E2's backside. While use of two subunits to recruit the E2 serves to ensure specificity for Ube2C, the additional interaction also appears to direct substrate ubiquitylation by reducing the degrees of freedom available for the E2/RING assembly
additional information
E2 structure-function analysis, overview. Multi-subunit E3s make use of the E2 backside surface. The APC/C engages Ube2C using both a RING subunit Apc11 and the WHB domain of a cullin subunit Apc2, the latter interaction being via the E2's backside. While use of two subunits to recruit the E2 serves to ensure specificity for Ube2C, the additional interaction also appears to direct substrate ubiquitylation by reducing the degrees of freedom available for the E2/RING assembly
additional information
E2 structure-function analysis, overview. Multi-subunit E3s make use of the E2 backside surface. The APC/C engages Ube2C using both a RING subunit Apc11 and the WHB domain of a cullin subunit Apc2, the latter interaction being via the E2's backside. While use of two subunits to recruit the E2 serves to ensure specificity for Ube2C, the additional interaction also appears to direct substrate ubiquitylation by reducing the degrees of freedom available for the E2/RING assembly
additional information
E2 structure-function analysis, overview. Multi-subunit E3s make use of the E2 backside surface. The APC/C engages Ube2C using both a RING subunit Apc11 and the WHB domain of a cullin subunit Apc2, the latter interaction being via the E2's backside. While use of two subunits to recruit the E2 serves to ensure specificity for Ube2C, the additional interaction also appears to direct substrate ubiquitylation by reducing the degrees of freedom available for the E2/RING assembly
additional information
E2 structure-function analysis, overview. Multi-subunit E3s make use of the E2 backside surface. The APC/C engages Ube2C using both a RING subunit Apc11 and the WHB domain of a cullin subunit Apc2, the latter interaction being via the E2's backside. While use of two subunits to recruit the E2 serves to ensure specificity for Ube2C, the additional interaction also appears to direct substrate ubiquitylation by reducing the degrees of freedom available for the E2/RING assembly
additional information
E2 structure-function analysis, overview. Multi-subunit E3s make use of the E2 backside surface. The APC/C engages Ube2C using both a RING subunit Apc11 and the WHB domain of a cullin subunit Apc2, the latter interaction being via the E2's backside. While use of two subunits to recruit the E2 serves to ensure specificity for Ube2C, the additional interaction also appears to direct substrate ubiquitylation by reducing the degrees of freedom available for the E2/RING assembly
additional information
E2 structure-function analysis, overview. Multi-subunit E3s make use of the E2 backside surface. The APC/C engages Ube2C using both a RING subunit Apc11 and the WHB domain of a cullin subunit Apc2, the latter interaction being via the E2's backside. While use of two subunits to recruit the E2 serves to ensure specificity for Ube2C, the additional interaction also appears to direct substrate ubiquitylation by reducing the degrees of freedom available for the E2/RING assembly
additional information
E2 structure-function analysis, overview. Multi-subunit E3s make use of the E2 backside surface. The APC/C engages Ube2C using both a RING subunit Apc11 and the WHB domain of a cullin subunit Apc2, the latter interaction being via the E2's backside. While use of two subunits to recruit the E2 serves to ensure specificity for Ube2C, the additional interaction also appears to direct substrate ubiquitylation by reducing the degrees of freedom available for the E2/RING assembly
additional information
E2 structure-function analysis, overview. Multi-subunit E3s make use of the E2 backside surface. The APC/C engages Ube2C using both a RING subunit Apc11 and the WHB domain of a cullin subunit Apc2, the latter interaction being via the E2's backside. While use of two subunits to recruit the E2 serves to ensure specificity for Ube2C, the additional interaction also appears to direct substrate ubiquitylation by reducing the degrees of freedom available for the E2/RING assembly
additional information
E2 structure-function analysis, overview. Multi-subunit E3s make use of the E2 backside surface. The APC/C engages Ube2C using both a RING subunit Apc11 and the WHB domain of a cullin subunit Apc2, the latter interaction being via the E2's backside. While use of two subunits to recruit the E2 serves to ensure specificity for Ube2C, the additional interaction also appears to direct substrate ubiquitylation by reducing the degrees of freedom available for the E2/RING assembly
additional information
E2 structure-function analysis, overview. Multi-subunit E3s make use of the E2 backside surface. The APC/C engages Ube2C using both a RING subunit Apc11 and the WHB domain of a cullin subunit Apc2, the latter interaction being via the E2's backside. While use of two subunits to recruit the E2 serves to ensure specificity for Ube2C, the additional interaction also appears to direct substrate ubiquitylation by reducing the degrees of freedom available for the E2/RING assembly
additional information
E2 structure-function analysis, overview. Multi-subunit E3s make use of the E2 backside surface. The APC/C engages Ube2C using both a RING subunit Apc11 and the WHB domain of a cullin subunit Apc2, the latter interaction being via the E2's backside. While use of two subunits to recruit the E2 serves to ensure specificity for Ube2C, the additional interaction also appears to direct substrate ubiquitylation by reducing the degrees of freedom available for the E2/RING assembly
additional information
E2 structure-function analysis, overview. Multi-subunit E3s make use of the E2 backside surface. The APC/C engages Ube2C using both a RING subunit Apc11 and the WHB domain of a cullin subunit Apc2, the latter interaction being via the E2's backside. While use of two subunits to recruit the E2 serves to ensure specificity for Ube2C, the additional interaction also appears to direct substrate ubiquitylation by reducing the degrees of freedom available for the E2/RING assembly
additional information
E2 structure-function analysis, overview. Multi-subunit E3s make use of the E2 backside surface. The APC/C engages Ube2C using both a RING subunit Apc11 and the WHB domain of a cullin subunit Apc2, the latter interaction being via the E2's backside. While use of two subunits to recruit the E2 serves to ensure specificity for Ube2C, the additional interaction also appears to direct substrate ubiquitylation by reducing the degrees of freedom available for the E2/RING assembly
additional information
E2 structure-function analysis, overview. Multi-subunit E3s make use of the E2 backside surface. The APC/C engages Ube2C using both a RING subunit Apc11 and the WHB domain of a cullin subunit Apc2, the latter interaction being via the E2's backside. While use of two subunits to recruit the E2 serves to ensure specificity for Ube2C, the additional interaction also appears to direct substrate ubiquitylation by reducing the degrees of freedom available for the E2/RING assembly
additional information
E2 structure-function analysis, overview. Multi-subunit E3s make use of the E2 backside surface. The APC/C engages Ube2C using both a RING subunit Apc11 and the WHB domain of a cullin subunit Apc2, the latter interaction being via the E2's backside. While use of two subunits to recruit the E2 serves to ensure specificity for Ube2C, the additional interaction also appears to direct substrate ubiquitylation by reducing the degrees of freedom available for the E2/RING assembly
additional information
E2 structure-function analysis, overview. Multi-subunit E3s make use of the E2 backside surface. The APC/C engages Ube2C using both a RING subunit Apc11 and the WHB domain of a cullin subunit Apc2, the latter interaction being via the E2's backside. While use of two subunits to recruit the E2 serves to ensure specificity for Ube2C, the additional interaction also appears to direct substrate ubiquitylation by reducing the degrees of freedom available for the E2/RING assembly
additional information
E2 structure-function analysis, overview. Multi-subunit E3s make use of the E2 backside surface. The APC/C engages Ube2C using both a RING subunit Apc11 and the WHB domain of a cullin subunit Apc2, the latter interaction being via the E2's backside. While use of two subunits to recruit the E2 serves to ensure specificity for Ube2C, the additional interaction also appears to direct substrate ubiquitylation by reducing the degrees of freedom available for the E2/RING assembly
additional information
E2 structure-function analysis, overview. Multi-subunit E3s make use of the E2 backside surface. The APC/C engages Ube2C using both a RING subunit Apc11 and the WHB domain of a cullin subunit Apc2, the latter interaction being via the E2's backside. While use of two subunits to recruit the E2 serves to ensure specificity for Ube2C, the additional interaction also appears to direct substrate ubiquitylation by reducing the degrees of freedom available for the E2/RING assembly
additional information
E2 structure-function analysis, overview. Multi-subunit E3s make use of the E2 backside surface. The APC/C engages Ube2C using both a RING subunit Apc11 and the WHB domain of a cullin subunit Apc2, the latter interaction being via the E2's backside. While use of two subunits to recruit the E2 serves to ensure specificity for Ube2C, the additional interaction also appears to direct substrate ubiquitylation by reducing the degrees of freedom available for the E2/RING assembly
additional information
E2 structure-function analysis, overview. Multi-subunit E3s make use of the E2 backside surface. The APC/C engages Ube2C using both a RING subunit Apc11 and the WHB domain of a cullin subunit Apc2, the latter interaction being via the E2's backside. While use of two subunits to recruit the E2 serves to ensure specificity for Ube2C, the additional interaction also appears to direct substrate ubiquitylation by reducing the degrees of freedom available for the E2/RING assembly
additional information
E2 structure-function analysis, overview. Structures of E2-Ub bound to a HECT (NEDD4L) or RBR (HOIP) E3 reveal a Ube2D2-Ub conjugate in an open conformation, poised for transthiolation to the E3 active-site cysteine
additional information
E2 structure-function analysis, overview. Structures of E2-Ub bound to a HECT (NEDD4L) or RBR (HOIP) E3 reveal a Ube2D2-Ub conjugate in an open conformation, poised for transthiolation to the E3 active-site cysteine
additional information
E2 structure-function analysis, overview. Structures of E2-Ub bound to a HECT (NEDD4L) or RBR (HOIP) E3 reveal a Ube2D2-Ub conjugate in an open conformation, poised for transthiolation to the E3 active-site cysteine
additional information
E2 structure-function analysis, overview. Structures of E2-Ub bound to a HECT (NEDD4L) or RBR (HOIP) E3 reveal a Ube2D2-Ub conjugate in an open conformation, poised for transthiolation to the E3 active-site cysteine
additional information
E2 structure-function analysis, overview. Structures of E2-Ub bound to a HECT (NEDD4L) or RBR (HOIP) E3 reveal a Ube2D2-Ub conjugate in an open conformation, poised for transthiolation to the E3 active-site cysteine
additional information
E2 structure-function analysis, overview. Structures of E2-Ub bound to a HECT (NEDD4L) or RBR (HOIP) E3 reveal a Ube2D2-Ub conjugate in an open conformation, poised for transthiolation to the E3 active-site cysteine
additional information
E2 structure-function analysis, overview. Structures of E2-Ub bound to a HECT (NEDD4L) or RBR (HOIP) E3 reveal a Ube2D2-Ub conjugate in an open conformation, poised for transthiolation to the E3 active-site cysteine
additional information
E2 structure-function analysis, overview. Structures of E2-Ub bound to a HECT (NEDD4L) or RBR (HOIP) E3 reveal a Ube2D2-Ub conjugate in an open conformation, poised for transthiolation to the E3 active-site cysteine
additional information
E2 structure-function analysis, overview. Structures of E2-Ub bound to a HECT (NEDD4L) or RBR (HOIP) E3 reveal a Ube2D2-Ub conjugate in an open conformation, poised for transthiolation to the E3 active-site cysteine
additional information
E2 structure-function analysis, overview. Structures of E2-Ub bound to a HECT (NEDD4L) or RBR (HOIP) E3 reveal a Ube2D2-Ub conjugate in an open conformation, poised for transthiolation to the E3 active-site cysteine
additional information
E2 structure-function analysis, overview. Structures of E2-Ub bound to a HECT (NEDD4L) or RBR (HOIP) E3 reveal a Ube2D2-Ub conjugate in an open conformation, poised for transthiolation to the E3 active-site cysteine
additional information
E2 structure-function analysis, overview. Structures of E2-Ub bound to a HECT (NEDD4L) or RBR (HOIP) E3 reveal a Ube2D2-Ub conjugate in an open conformation, poised for transthiolation to the E3 active-site cysteine
additional information
E2 structure-function analysis, overview. Structures of E2-Ub bound to a HECT (NEDD4L) or RBR (HOIP) E3 reveal a Ube2D2-Ub conjugate in an open conformation, poised for transthiolation to the E3 active-site cysteine
additional information
E2 structure-function analysis, overview. Structures of E2-Ub bound to a HECT (NEDD4L) or RBR (HOIP) E3 reveal a Ube2D2-Ub conjugate in an open conformation, poised for transthiolation to the E3 active-site cysteine
additional information
E2 structure-function analysis, overview. Structures of E2-Ub bound to a HECT (NEDD4L) or RBR (HOIP) E3 reveal a Ube2D2-Ub conjugate in an open conformation, poised for transthiolation to the E3 active-site cysteine
additional information
E2 structure-function analysis, overview. Structures of E2-Ub bound to a HECT (NEDD4L) or RBR (HOIP) E3 reveal a Ube2D2-Ub conjugate in an open conformation, poised for transthiolation to the E3 active-site cysteine
additional information
E2 structure-function analysis, overview. Structures of E2-Ub bound to a HECT (NEDD4L) or RBR (HOIP) E3 reveal a Ube2D2-Ub conjugate in an open conformation, poised for transthiolation to the E3 active-site cysteine
additional information
E2 structure-function analysis, overview. Structures of E2-Ub bound to a HECT (NEDD4L) or RBR (HOIP) E3 reveal a Ube2D2-Ub conjugate in an open conformation, poised for transthiolation to the E3 active-site cysteine
additional information
E2 structure-function analysis, overview. Structures of E2-Ub bound to a HECT (NEDD4L) or RBR (HOIP) E3 reveal a Ube2D2-Ub conjugate in an open conformation, poised for transthiolation to the E3 active-site cysteine
additional information
E2 structure-function analysis, overview. Structures of E2-Ub bound to a HECT (NEDD4L) or RBR (HOIP) E3 reveal a Ube2D2-Ub conjugate in an open conformation, poised for transthiolation to the E3 active-site cysteine
additional information
E2 structure-function analysis, overview. Structures of E2-Ub bound to a HECT (NEDD4L) or RBR (HOIP) E3 reveal a Ube2D2-Ub conjugate in an open conformation, poised for transthiolation to the E3 active-site cysteine
additional information
E2 structure-function analysis, overview. Structures of E2-Ub bound to a HECT (NEDD4L) or RBR (HOIP) E3 reveal a Ube2D2-Ub conjugate in an open conformation, poised for transthiolation to the E3 active-site cysteine
additional information
E2 structure-function analysis, overview. Structures of E2-Ub bound to a HECT (NEDD4L) or RBR (HOIP) E3 reveal a Ube2D2-Ub conjugate in an open conformation, poised for transthiolation to the E3 active-site cysteine
additional information
E2 structure-function analysis, overview. Structures of E2-Ub bound to a HECT (NEDD4L) or RBR (HOIP) E3 reveal a Ube2D2-Ub conjugate in an open conformation, poised for transthiolation to the E3 active-site cysteine
additional information
E2 structure-function analysis, overview. Structures of E2-Ub bound to a HECT (NEDD4L) or RBR (HOIP) E3 reveal a Ube2D2-Ub conjugate in an open conformation, poised for transthiolation to the E3 active-site cysteine
additional information
E2 structure-function analysis, overview. Structures of E2-Ub bound to a HECT (NEDD4L) or RBR (HOIP) E3 reveal a Ube2D2-Ub conjugate in an open conformation, poised for transthiolation to the E3 active-site cysteine
additional information
E2 structure-function analysis, overview. Structures of E2-Ub bound to a HECT (NEDD4L) or RBR (HOIP) E3 reveal a Ube2D2-Ub conjugate in an open conformation, poised for transthiolation to the E3 active-site cysteine
additional information
E2 structure-function analysis, overview. Structures of E2-Ub bound to a HECT (NEDD4L) or RBR (HOIP) E3 reveal a Ube2D2-Ub conjugate in an open conformation, poised for transthiolation to the E3 active-site cysteine
additional information
E2 structure-function analysis, overview. Structures of E2-Ub bound to a HECT (NEDD4L) or RBR (HOIP) E3 reveal a Ube2D2-Ub conjugate in an open conformation, poised for transthiolation to the E3 active-site cysteine
additional information
E2 structure-function analysis, overview. Structures of E2-Ub bound to a HECT (NEDD4L) or RBR (HOIP) E3 reveal a Ube2D2-Ub conjugate in an open conformation, poised for transthiolation to the E3 active-site cysteine
additional information
E2 structure-function analysis, overview. Ube2D3-Ub and Ube2N-Ub conjugates show an array of orientations that involve little or no contact between the E2 and ubiquitin (open states) and some conformations (closed states) that involve contacts between the Ub hydrophobic patch centered on Ub I44 and residues in the E2 crossover helix. Although Ube2D3-Ub and Ube2N-Ub conjugates are highly dynamic, the ensembles of conformations adopted by them are different in terms of the relative fraction of closed versus open states
additional information
E2 structure-function analysis, overview. Ube2D3-Ub and Ube2N-Ub conjugates show an array of orientations that involve little or no contact between the E2 and ubiquitin (open states) and some conformations (closed states) that involve contacts between the Ub hydrophobic patch centered on Ub I44 and residues in the E2 crossover helix. Although Ube2D3-Ub and Ube2N-Ub conjugates are highly dynamic, the ensembles of conformations adopted by them are different in terms of the relative fraction of closed versus open states
additional information
E2 structure-function analysis, overview. Ube2D3-Ub and Ube2N-Ub conjugates show an array of orientations that involve little or no contact between the E2 and ubiquitin (open states) and some conformations (closed states) that involve contacts between the Ub hydrophobic patch centered on Ub I44 and residues in the E2 crossover helix. Although Ube2D3-Ub and Ube2N-Ub conjugates are highly dynamic, the ensembles of conformations adopted by them are different in terms of the relative fraction of closed versus open states
additional information
E2 structure-function analysis, overview. Ube2D3-Ub and Ube2N-Ub conjugates show an array of orientations that involve little or no contact between the E2 and ubiquitin (open states) and some conformations (closed states) that involve contacts between the Ub hydrophobic patch centered on Ub I44 and residues in the E2 crossover helix. Although Ube2D3-Ub and Ube2N-Ub conjugates are highly dynamic, the ensembles of conformations adopted by them are different in terms of the relative fraction of closed versus open states
additional information
E2 structure-function analysis, overview. Ube2D3-Ub and Ube2N-Ub conjugates show an array of orientations that involve little or no contact between the E2 and ubiquitin (open states) and some conformations (closed states) that involve contacts between the Ub hydrophobic patch centered on Ub I44 and residues in the E2 crossover helix. Although Ube2D3-Ub and Ube2N-Ub conjugates are highly dynamic, the ensembles of conformations adopted by them are different in terms of the relative fraction of closed versus open states
additional information
E2 structure-function analysis, overview. Ube2D3-Ub and Ube2N-Ub conjugates show an array of orientations that involve little or no contact between the E2 and ubiquitin (open states) and some conformations (closed states) that involve contacts between the Ub hydrophobic patch centered on Ub I44 and residues in the E2 crossover helix. Although Ube2D3-Ub and Ube2N-Ub conjugates are highly dynamic, the ensembles of conformations adopted by them are different in terms of the relative fraction of closed versus open states
additional information
E2 structure-function analysis, overview. Ube2D3-Ub and Ube2N-Ub conjugates show an array of orientations that involve little or no contact between the E2 and ubiquitin (open states) and some conformations (closed states) that involve contacts between the Ub hydrophobic patch centered on Ub I44 and residues in the E2 crossover helix. Although Ube2D3-Ub and Ube2N-Ub conjugates are highly dynamic, the ensembles of conformations adopted by them are different in terms of the relative fraction of closed versus open states
additional information
E2 structure-function analysis, overview. Ube2D3-Ub and Ube2N-Ub conjugates show an array of orientations that involve little or no contact between the E2 and ubiquitin (open states) and some conformations (closed states) that involve contacts between the Ub hydrophobic patch centered on Ub I44 and residues in the E2 crossover helix. Although Ube2D3-Ub and Ube2N-Ub conjugates are highly dynamic, the ensembles of conformations adopted by them are different in terms of the relative fraction of closed versus open states
additional information
E2 structure-function analysis, overview. Ube2D3-Ub and Ube2N-Ub conjugates show an array of orientations that involve little or no contact between the E2 and ubiquitin (open states) and some conformations (closed states) that involve contacts between the Ub hydrophobic patch centered on Ub I44 and residues in the E2 crossover helix. Although Ube2D3-Ub and Ube2N-Ub conjugates are highly dynamic, the ensembles of conformations adopted by them are different in terms of the relative fraction of closed versus open states
additional information
E2 structure-function analysis, overview. Ube2D3-Ub and Ube2N-Ub conjugates show an array of orientations that involve little or no contact between the E2 and ubiquitin (open states) and some conformations (closed states) that involve contacts between the Ub hydrophobic patch centered on Ub I44 and residues in the E2 crossover helix. Although Ube2D3-Ub and Ube2N-Ub conjugates are highly dynamic, the ensembles of conformations adopted by them are different in terms of the relative fraction of closed versus open states
additional information
E2 structure-function analysis, overview. Ube2D3-Ub and Ube2N-Ub conjugates show an array of orientations that involve little or no contact between the E2 and ubiquitin (open states) and some conformations (closed states) that involve contacts between the Ub hydrophobic patch centered on Ub I44 and residues in the E2 crossover helix. Although Ube2D3-Ub and Ube2N-Ub conjugates are highly dynamic, the ensembles of conformations adopted by them are different in terms of the relative fraction of closed versus open states
additional information
E2 structure-function analysis, overview. Ube2D3-Ub and Ube2N-Ub conjugates show an array of orientations that involve little or no contact between the E2 and ubiquitin (open states) and some conformations (closed states) that involve contacts between the Ub hydrophobic patch centered on Ub I44 and residues in the E2 crossover helix. Although Ube2D3-Ub and Ube2N-Ub conjugates are highly dynamic, the ensembles of conformations adopted by them are different in terms of the relative fraction of closed versus open states
additional information
E2 structure-function analysis, overview. Ube2D3-Ub and Ube2N-Ub conjugates show an array of orientations that involve little or no contact between the E2 and ubiquitin (open states) and some conformations (closed states) that involve contacts between the Ub hydrophobic patch centered on Ub I44 and residues in the E2 crossover helix. Although Ube2D3-Ub and Ube2N-Ub conjugates are highly dynamic, the ensembles of conformations adopted by them are different in terms of the relative fraction of closed versus open states
additional information
E2 structure-function analysis, overview. Ube2D3-Ub and Ube2N-Ub conjugates show an array of orientations that involve little or no contact between the E2 and ubiquitin (open states) and some conformations (closed states) that involve contacts between the Ub hydrophobic patch centered on Ub I44 and residues in the E2 crossover helix. Although Ube2D3-Ub and Ube2N-Ub conjugates are highly dynamic, the ensembles of conformations adopted by them are different in terms of the relative fraction of closed versus open states
additional information
E2 structure-function analysis, overview. Ube2D3-Ub and Ube2N-Ub conjugates show an array of orientations that involve little or no contact between the E2 and ubiquitin (open states) and some conformations (closed states) that involve contacts between the Ub hydrophobic patch centered on Ub I44 and residues in the E2 crossover helix. Although Ube2D3-Ub and Ube2N-Ub conjugates are highly dynamic, the ensembles of conformations adopted by them are different in terms of the relative fraction of closed versus open states
additional information
E2 structure-function analysis, overview. Ube2D3-Ub and Ube2N-Ub conjugates show an array of orientations that involve little or no contact between the E2 and ubiquitin (open states) and some conformations (closed states) that involve contacts between the Ub hydrophobic patch centered on Ub I44 and residues in the E2 crossover helix. Although Ube2D3-Ub and Ube2N-Ub conjugates are highly dynamic, the ensembles of conformations adopted by them are different in terms of the relative fraction of closed versus open states
additional information
E2 structure-function analysis, overview. Ube2D3-Ub and Ube2N-Ub conjugates show an array of orientations that involve little or no contact between the E2 and ubiquitin (open states) and some conformations (closed states) that involve contacts between the Ub hydrophobic patch centered on Ub I44 and residues in the E2 crossover helix. Although Ube2D3-Ub and Ube2N-Ub conjugates are highly dynamic, the ensembles of conformations adopted by them are different in terms of the relative fraction of closed versus open states
additional information
E2 structure-function analysis, overview. Ube2D3-Ub and Ube2N-Ub conjugates show an array of orientations that involve little or no contact between the E2 and ubiquitin (open states) and some conformations (closed states) that involve contacts between the Ub hydrophobic patch centered on Ub I44 and residues in the E2 crossover helix. Although Ube2D3-Ub and Ube2N-Ub conjugates are highly dynamic, the ensembles of conformations adopted by them are different in terms of the relative fraction of closed versus open states
additional information
E2 structure-function analysis, overview. Ube2D3-Ub and Ube2N-Ub conjugates show an array of orientations that involve little or no contact between the E2 and ubiquitin (open states) and some conformations (closed states) that involve contacts between the Ub hydrophobic patch centered on Ub I44 and residues in the E2 crossover helix. Although Ube2D3-Ub and Ube2N-Ub conjugates are highly dynamic, the ensembles of conformations adopted by them are different in terms of the relative fraction of closed versus open states
additional information
E2 structure-function analysis, overview. Ube2D3-Ub and Ube2N-Ub conjugates show an array of orientations that involve little or no contact between the E2 and ubiquitin (open states) and some conformations (closed states) that involve contacts between the Ub hydrophobic patch centered on Ub I44 and residues in the E2 crossover helix. Although Ube2D3-Ub and Ube2N-Ub conjugates are highly dynamic, the ensembles of conformations adopted by them are different in terms of the relative fraction of closed versus open states
additional information
E2 structure-function analysis, overview. Ube2D3-Ub and Ube2N-Ub conjugates show an array of orientations that involve little or no contact between the E2 and ubiquitin (open states) and some conformations (closed states) that involve contacts between the Ub hydrophobic patch centered on Ub I44 and residues in the E2 crossover helix. Although Ube2D3-Ub and Ube2N-Ub conjugates are highly dynamic, the ensembles of conformations adopted by them are different in terms of the relative fraction of closed versus open states
additional information
E2 structure-function analysis, overview. Ube2D3-Ub and Ube2N-Ub conjugates show an array of orientations that involve little or no contact between the E2 and ubiquitin (open states) and some conformations (closed states) that involve contacts between the Ub hydrophobic patch centered on Ub I44 and residues in the E2 crossover helix. Although Ube2D3-Ub and Ube2N-Ub conjugates are highly dynamic, the ensembles of conformations adopted by them are different in terms of the relative fraction of closed versus open states
additional information
E2 structure-function analysis, overview. Ube2D3-Ub and Ube2N-Ub conjugates show an array of orientations that involve little or no contact between the E2 and ubiquitin (open states) and some conformations (closed states) that involve contacts between the Ub hydrophobic patch centered on Ub I44 and residues in the E2 crossover helix. Although Ube2D3-Ub and Ube2N-Ub conjugates are highly dynamic, the ensembles of conformations adopted by them are different in terms of the relative fraction of closed versus open states
additional information
E2 structure-function analysis, overview. Ube2D3-Ub and Ube2N-Ub conjugates show an array of orientations that involve little or no contact between the E2 and ubiquitin (open states) and some conformations (closed states) that involve contacts between the Ub hydrophobic patch centered on Ub I44 and residues in the E2 crossover helix. Although Ube2D3-Ub and Ube2N-Ub conjugates are highly dynamic, the ensembles of conformations adopted by them are different in terms of the relative fraction of closed versus open states
additional information
E2 structure-function analysis, overview. Ube2D3-Ub and Ube2N-Ub conjugates show an array of orientations that involve little or no contact between the E2 and ubiquitin (open states) and some conformations (closed states) that involve contacts between the Ub hydrophobic patch centered on Ub I44 and residues in the E2 crossover helix. Although Ube2D3-Ub and Ube2N-Ub conjugates are highly dynamic, the ensembles of conformations adopted by them are different in terms of the relative fraction of closed versus open states
additional information
E2 structure-function analysis, overview. Ube2D3-Ub and Ube2N-Ub conjugates show an array of orientations that involve little or no contact between the E2 and ubiquitin (open states) and some conformations (closed states) that involve contacts between the Ub hydrophobic patch centered on Ub I44 and residues in the E2 crossover helix. Although Ube2D3-Ub and Ube2N-Ub conjugates are highly dynamic, the ensembles of conformations adopted by them are different in terms of the relative fraction of closed versus open states
additional information
E2 structure-function analysis, overview. Ube2D3-Ub and Ube2N-Ub conjugates show an array of orientations that involve little or no contact between the E2 and ubiquitin (open states) and some conformations (closed states) that involve contacts between the Ub hydrophobic patch centered on Ub I44 and residues in the E2 crossover helix. Although Ube2D3-Ub and Ube2N-Ub conjugates are highly dynamic, the ensembles of conformations adopted by them are different in terms of the relative fraction of closed versus open states
additional information
E2 structure-function analysis, overview. Ube2D3-Ub and Ube2N-Ub conjugates show an array of orientations that involve little or no contact between the E2 and ubiquitin (open states) and some conformations (closed states) that involve contacts between the Ub hydrophobic patch centered on Ub I44 and residues in the E2 crossover helix. Although Ube2D3-Ub and Ube2N-Ub conjugates are highly dynamic, the ensembles of conformations adopted by them are different in terms of the relative fraction of closed versus open states
additional information
E2 structure-function analysis, overview. Ube2D3-Ub and Ube2N-Ub conjugates show an array of orientations that involve little or no contact between the E2 and ubiquitin (open states) and some conformations (closed states) that involve contacts between the Ub hydrophobic patch centered on Ub I44 and residues in the E2 crossover helix. Although Ube2D3-Ub and Ube2N-Ub conjugates are highly dynamic, the ensembles of conformations adopted by them are different in terms of the relative fraction of closed versus open states
additional information
E2 structure-function analysis, overview. Ube2D3-Ub and Ube2N-Ub conjugates show an array of orientations that involve little or no contact between the E2 and ubiquitin (open states) and some conformations (closed states) that involve contacts between the Ub hydrophobic patch centered on Ub I44 and residues in the E2 crossover helix. Although Ube2D3-Ub and Ube2N-Ub conjugates are highly dynamic, the ensembles of conformations adopted by them are different in terms of the relative fraction of closed versus open states
additional information
E2 structure-function analysis, overview. UBE2E3 can be thought of having an intrinsic ability to build polyUb chains that is inhibited by Ub binding on its backside. The two opposite effects of backside Ub binding suggest that it can act as either a throttle or a brake for chain building
additional information
E2 structure-function analysis, overview. UBE2E3 can be thought of having an intrinsic ability to build polyUb chains that is inhibited by Ub binding on its backside. The two opposite effects of backside Ub binding suggest that it can act as either a throttle or a brake for chain building
additional information
E2 structure-function analysis, overview. UBE2E3 can be thought of having an intrinsic ability to build polyUb chains that is inhibited by Ub binding on its backside. The two opposite effects of backside Ub binding suggest that it can act as either a throttle or a brake for chain building
additional information
E2 structure-function analysis, overview. UBE2E3 can be thought of having an intrinsic ability to build polyUb chains that is inhibited by Ub binding on its backside. The two opposite effects of backside Ub binding suggest that it can act as either a throttle or a brake for chain building
additional information
E2 structure-function analysis, overview. UBE2E3 can be thought of having an intrinsic ability to build polyUb chains that is inhibited by Ub binding on its backside. The two opposite effects of backside Ub binding suggest that it can act as either a throttle or a brake for chain building
additional information
E2 structure-function analysis, overview. UBE2E3 can be thought of having an intrinsic ability to build polyUb chains that is inhibited by Ub binding on its backside. The two opposite effects of backside Ub binding suggest that it can act as either a throttle or a brake for chain building
additional information
E2 structure-function analysis, overview. UBE2E3 can be thought of having an intrinsic ability to build polyUb chains that is inhibited by Ub binding on its backside. The two opposite effects of backside Ub binding suggest that it can act as either a throttle or a brake for chain building
additional information
E2 structure-function analysis, overview. UBE2E3 can be thought of having an intrinsic ability to build polyUb chains that is inhibited by Ub binding on its backside. The two opposite effects of backside Ub binding suggest that it can act as either a throttle or a brake for chain building
additional information
E2 structure-function analysis, overview. UBE2E3 can be thought of having an intrinsic ability to build polyUb chains that is inhibited by Ub binding on its backside. The two opposite effects of backside Ub binding suggest that it can act as either a throttle or a brake for chain building
additional information
E2 structure-function analysis, overview. UBE2E3 can be thought of having an intrinsic ability to build polyUb chains that is inhibited by Ub binding on its backside. The two opposite effects of backside Ub binding suggest that it can act as either a throttle or a brake for chain building
additional information
E2 structure-function analysis, overview. UBE2E3 can be thought of having an intrinsic ability to build polyUb chains that is inhibited by Ub binding on its backside. The two opposite effects of backside Ub binding suggest that it can act as either a throttle or a brake for chain building
additional information
E2 structure-function analysis, overview. UBE2E3 can be thought of having an intrinsic ability to build polyUb chains that is inhibited by Ub binding on its backside. The two opposite effects of backside Ub binding suggest that it can act as either a throttle or a brake for chain building
additional information
E2 structure-function analysis, overview. UBE2E3 can be thought of having an intrinsic ability to build polyUb chains that is inhibited by Ub binding on its backside. The two opposite effects of backside Ub binding suggest that it can act as either a throttle or a brake for chain building
additional information
E2 structure-function analysis, overview. UBE2E3 can be thought of having an intrinsic ability to build polyUb chains that is inhibited by Ub binding on its backside. The two opposite effects of backside Ub binding suggest that it can act as either a throttle or a brake for chain building
additional information
E2 structure-function analysis, overview. UBE2E3 can be thought of having an intrinsic ability to build polyUb chains that is inhibited by Ub binding on its backside. The two opposite effects of backside Ub binding suggest that it can act as either a throttle or a brake for chain building
additional information
E2 structure-function analysis, overview. UBE2E3 can be thought of having an intrinsic ability to build polyUb chains that is inhibited by Ub binding on its backside. The two opposite effects of backside Ub binding suggest that it can act as either a throttle or a brake for chain building
additional information
E2 structure-function analysis, overview. UBE2E3 can be thought of having an intrinsic ability to build polyUb chains that is inhibited by Ub binding on its backside. The two opposite effects of backside Ub binding suggest that it can act as either a throttle or a brake for chain building
additional information
E2 structure-function analysis, overview. UBE2E3 can be thought of having an intrinsic ability to build polyUb chains that is inhibited by Ub binding on its backside. The two opposite effects of backside Ub binding suggest that it can act as either a throttle or a brake for chain building
additional information
E2 structure-function analysis, overview. UBE2E3 can be thought of having an intrinsic ability to build polyUb chains that is inhibited by Ub binding on its backside. The two opposite effects of backside Ub binding suggest that it can act as either a throttle or a brake for chain building
additional information
E2 structure-function analysis, overview. UBE2E3 can be thought of having an intrinsic ability to build polyUb chains that is inhibited by Ub binding on its backside. The two opposite effects of backside Ub binding suggest that it can act as either a throttle or a brake for chain building
additional information
E2 structure-function analysis, overview. UBE2E3 can be thought of having an intrinsic ability to build polyUb chains that is inhibited by Ub binding on its backside. The two opposite effects of backside Ub binding suggest that it can act as either a throttle or a brake for chain building
additional information
E2 structure-function analysis, overview. UBE2E3 can be thought of having an intrinsic ability to build polyUb chains that is inhibited by Ub binding on its backside. The two opposite effects of backside Ub binding suggest that it can act as either a throttle or a brake for chain building
additional information
E2 structure-function analysis, overview. UBE2E3 can be thought of having an intrinsic ability to build polyUb chains that is inhibited by Ub binding on its backside. The two opposite effects of backside Ub binding suggest that it can act as either a throttle or a brake for chain building
additional information
E2 structure-function analysis, overview. UBE2E3 can be thought of having an intrinsic ability to build polyUb chains that is inhibited by Ub binding on its backside. The two opposite effects of backside Ub binding suggest that it can act as either a throttle or a brake for chain building
additional information
E2 structure-function analysis, overview. UBE2E3 can be thought of having an intrinsic ability to build polyUb chains that is inhibited by Ub binding on its backside. The two opposite effects of backside Ub binding suggest that it can act as either a throttle or a brake for chain building
additional information
E2 structure-function analysis, overview. UBE2E3 can be thought of having an intrinsic ability to build polyUb chains that is inhibited by Ub binding on its backside. The two opposite effects of backside Ub binding suggest that it can act as either a throttle or a brake for chain building
additional information
E2 structure-function analysis, overview. UBE2E3 can be thought of having an intrinsic ability to build polyUb chains that is inhibited by Ub binding on its backside. The two opposite effects of backside Ub binding suggest that it can act as either a throttle or a brake for chain building
additional information
E2 structure-function analysis, overview. UBE2E3 can be thought of having an intrinsic ability to build polyUb chains that is inhibited by Ub binding on its backside. The two opposite effects of backside Ub binding suggest that it can act as either a throttle or a brake for chain building
additional information
E2 structure-function analysis, overview. UBE2E3 can be thought of having an intrinsic ability to build polyUb chains that is inhibited by Ub binding on its backside. The two opposite effects of backside Ub binding suggest that it can act as either a throttle or a brake for chain building
additional information
E2 structure-function analysis, overview. UBE2E3 can be thought of having an intrinsic ability to build polyUb chains that is inhibited by Ub binding on its backside. The two opposite effects of backside Ub binding suggest that it can act as either a throttle or a brake for chain building
additional information
E2 structure-function analysis, overview. Ube2G1 has a short about 12 amino acid insertion proximal to the E2 active site that determines specificity
additional information
E2 structure-function analysis, overview. Ube2G1 has a short about 12 amino acid insertion proximal to the E2 active site that determines specificity
additional information
E2 structure-function analysis, overview. Ube2G1 has a short about 12 amino acid insertion proximal to the E2 active site that determines specificity
additional information
E2 structure-function analysis, overview. Ube2G1 has a short about 12 amino acid insertion proximal to the E2 active site that determines specificity
additional information
E2 structure-function analysis, overview. Ube2G1 has a short about 12 amino acid insertion proximal to the E2 active site that determines specificity
additional information
E2 structure-function analysis, overview. Ube2G1 has a short about 12 amino acid insertion proximal to the E2 active site that determines specificity
additional information
E2 structure-function analysis, overview. Ube2G1 has a short about 12 amino acid insertion proximal to the E2 active site that determines specificity
additional information
E2 structure-function analysis, overview. Ube2G1 has a short about 12 amino acid insertion proximal to the E2 active site that determines specificity
additional information
E2 structure-function analysis, overview. Ube2G1 has a short about 12 amino acid insertion proximal to the E2 active site that determines specificity
additional information
E2 structure-function analysis, overview. Ube2G1 has a short about 12 amino acid insertion proximal to the E2 active site that determines specificity
additional information
E2 structure-function analysis, overview. Ube2G1 has a short about 12 amino acid insertion proximal to the E2 active site that determines specificity
additional information
E2 structure-function analysis, overview. Ube2G1 has a short about 12 amino acid insertion proximal to the E2 active site that determines specificity
additional information
E2 structure-function analysis, overview. Ube2G1 has a short about 12 amino acid insertion proximal to the E2 active site that determines specificity
additional information
E2 structure-function analysis, overview. Ube2G1 has a short about 12 amino acid insertion proximal to the E2 active site that determines specificity
additional information
E2 structure-function analysis, overview. Ube2G1 has a short about 12 amino acid insertion proximal to the E2 active site that determines specificity
additional information
E2 structure-function analysis, overview. Ube2G1 has a short about 12 amino acid insertion proximal to the E2 active site that determines specificity
additional information
E2 structure-function analysis, overview. Ube2G1 has a short about 12 amino acid insertion proximal to the E2 active site that determines specificity
additional information
E2 structure-function analysis, overview. Ube2G1 has a short about 12 amino acid insertion proximal to the E2 active site that determines specificity
additional information
E2 structure-function analysis, overview. Ube2G1 has a short about 12 amino acid insertion proximal to the E2 active site that determines specificity
additional information
E2 structure-function analysis, overview. Ube2G1 has a short about 12 amino acid insertion proximal to the E2 active site that determines specificity
additional information
E2 structure-function analysis, overview. Ube2G1 has a short about 12 amino acid insertion proximal to the E2 active site that determines specificity
additional information
E2 structure-function analysis, overview. Ube2G1 has a short about 12 amino acid insertion proximal to the E2 active site that determines specificity
additional information
E2 structure-function analysis, overview. Ube2G1 has a short about 12 amino acid insertion proximal to the E2 active site that determines specificity
additional information
E2 structure-function analysis, overview. Ube2G1 has a short about 12 amino acid insertion proximal to the E2 active site that determines specificity
additional information
E2 structure-function analysis, overview. Ube2G1 has a short about 12 amino acid insertion proximal to the E2 active site that determines specificity
additional information
E2 structure-function analysis, overview. Ube2G1 has a short about 12 amino acid insertion proximal to the E2 active site that determines specificity
additional information
E2 structure-function analysis, overview. Ube2G1 has a short about 12 amino acid insertion proximal to the E2 active site that determines specificity
additional information
E2 structure-function analysis, overview. Ube2G1 has a short about 12 amino acid insertion proximal to the E2 active site that determines specificity
additional information
E2 structure-function analysis, overview. Ube2G1 has a short about 12 amino acid insertion proximal to the E2 active site that determines specificity
additional information
E2 structure-function analysis, overview. Ube2G1 has a short about 12 amino acid insertion proximal to the E2 active site that determines specificity
additional information
E2 structure-function analysis, overview. Ube2G2 has a short about 12 amino acid insertion proximal to the E2 active site that determines specificity. In the case of Ube2G2, binding of a non-RING region (G2BR) of its E3, gp78, to the backside of the UBC domain alters the acidic loop conformation, which is helical in the free E2 structure but is unwound in the G2BR-bound structure. The unwinding generates a series of interactions among E2, E3, and Ub that help stabilize a closed E2-Ub conformation to increase aminolysis reactivity. The requirement of an extra, allosteric interaction between Ube2G2 and gp78 ensures that the K48 chain-building E2 cannot work with any RING E3 it happens to contact. The human ERAD E3 ligase, gp78, uses the non-RING G2BR to interact with the backside of its E2, Ube2G2. G2BR binding in trans can increase the affinity of Ube2G2-Ub for the gp78 RING and can enhance both E3-dependent and E3-independent Ub transfer activity, suggesting cooperative allosteric interactions between RING and G2BR binding. The situation is different in the case of uncharged Ube2G2, which binds the E3 with lower affinity due to loss of some G2BR contacts, an effect that promotes dissociation of reacted (or inactive) E2 from the E3, allowing for exchange with active E2-Ub conjugate
additional information
E2 structure-function analysis, overview. Ube2G2 has a short about 12 amino acid insertion proximal to the E2 active site that determines specificity. In the case of Ube2G2, binding of a non-RING region (G2BR) of its E3, gp78, to the backside of the UBC domain alters the acidic loop conformation, which is helical in the free E2 structure but is unwound in the G2BR-bound structure. The unwinding generates a series of interactions among E2, E3, and Ub that help stabilize a closed E2-Ub conformation to increase aminolysis reactivity. The requirement of an extra, allosteric interaction between Ube2G2 and gp78 ensures that the K48 chain-building E2 cannot work with any RING E3 it happens to contact. The human ERAD E3 ligase, gp78, uses the non-RING G2BR to interact with the backside of its E2, Ube2G2. G2BR binding in trans can increase the affinity of Ube2G2-Ub for the gp78 RING and can enhance both E3-dependent and E3-independent Ub transfer activity, suggesting cooperative allosteric interactions between RING and G2BR binding. The situation is different in the case of uncharged Ube2G2, which binds the E3 with lower affinity due to loss of some G2BR contacts, an effect that promotes dissociation of reacted (or inactive) E2 from the E3, allowing for exchange with active E2-Ub conjugate
additional information
E2 structure-function analysis, overview. Ube2G2 has a short about 12 amino acid insertion proximal to the E2 active site that determines specificity. In the case of Ube2G2, binding of a non-RING region (G2BR) of its E3, gp78, to the backside of the UBC domain alters the acidic loop conformation, which is helical in the free E2 structure but is unwound in the G2BR-bound structure. The unwinding generates a series of interactions among E2, E3, and Ub that help stabilize a closed E2-Ub conformation to increase aminolysis reactivity. The requirement of an extra, allosteric interaction between Ube2G2 and gp78 ensures that the K48 chain-building E2 cannot work with any RING E3 it happens to contact. The human ERAD E3 ligase, gp78, uses the non-RING G2BR to interact with the backside of its E2, Ube2G2. G2BR binding in trans can increase the affinity of Ube2G2-Ub for the gp78 RING and can enhance both E3-dependent and E3-independent Ub transfer activity, suggesting cooperative allosteric interactions between RING and G2BR binding. The situation is different in the case of uncharged Ube2G2, which binds the E3 with lower affinity due to loss of some G2BR contacts, an effect that promotes dissociation of reacted (or inactive) E2 from the E3, allowing for exchange with active E2-Ub conjugate
additional information
E2 structure-function analysis, overview. Ube2G2 has a short about 12 amino acid insertion proximal to the E2 active site that determines specificity. In the case of Ube2G2, binding of a non-RING region (G2BR) of its E3, gp78, to the backside of the UBC domain alters the acidic loop conformation, which is helical in the free E2 structure but is unwound in the G2BR-bound structure. The unwinding generates a series of interactions among E2, E3, and Ub that help stabilize a closed E2-Ub conformation to increase aminolysis reactivity. The requirement of an extra, allosteric interaction between Ube2G2 and gp78 ensures that the K48 chain-building E2 cannot work with any RING E3 it happens to contact. The human ERAD E3 ligase, gp78, uses the non-RING G2BR to interact with the backside of its E2, Ube2G2. G2BR binding in trans can increase the affinity of Ube2G2-Ub for the gp78 RING and can enhance both E3-dependent and E3-independent Ub transfer activity, suggesting cooperative allosteric interactions between RING and G2BR binding. The situation is different in the case of uncharged Ube2G2, which binds the E3 with lower affinity due to loss of some G2BR contacts, an effect that promotes dissociation of reacted (or inactive) E2 from the E3, allowing for exchange with active E2-Ub conjugate
additional information
E2 structure-function analysis, overview. Ube2G2 has a short about 12 amino acid insertion proximal to the E2 active site that determines specificity. In the case of Ube2G2, binding of a non-RING region (G2BR) of its E3, gp78, to the backside of the UBC domain alters the acidic loop conformation, which is helical in the free E2 structure but is unwound in the G2BR-bound structure. The unwinding generates a series of interactions among E2, E3, and Ub that help stabilize a closed E2-Ub conformation to increase aminolysis reactivity. The requirement of an extra, allosteric interaction between Ube2G2 and gp78 ensures that the K48 chain-building E2 cannot work with any RING E3 it happens to contact. The human ERAD E3 ligase, gp78, uses the non-RING G2BR to interact with the backside of its E2, Ube2G2. G2BR binding in trans can increase the affinity of Ube2G2-Ub for the gp78 RING and can enhance both E3-dependent and E3-independent Ub transfer activity, suggesting cooperative allosteric interactions between RING and G2BR binding. The situation is different in the case of uncharged Ube2G2, which binds the E3 with lower affinity due to loss of some G2BR contacts, an effect that promotes dissociation of reacted (or inactive) E2 from the E3, allowing for exchange with active E2-Ub conjugate
additional information
E2 structure-function analysis, overview. Ube2G2 has a short about 12 amino acid insertion proximal to the E2 active site that determines specificity. In the case of Ube2G2, binding of a non-RING region (G2BR) of its E3, gp78, to the backside of the UBC domain alters the acidic loop conformation, which is helical in the free E2 structure but is unwound in the G2BR-bound structure. The unwinding generates a series of interactions among E2, E3, and Ub that help stabilize a closed E2-Ub conformation to increase aminolysis reactivity. The requirement of an extra, allosteric interaction between Ube2G2 and gp78 ensures that the K48 chain-building E2 cannot work with any RING E3 it happens to contact. The human ERAD E3 ligase, gp78, uses the non-RING G2BR to interact with the backside of its E2, Ube2G2. G2BR binding in trans can increase the affinity of Ube2G2-Ub for the gp78 RING and can enhance both E3-dependent and E3-independent Ub transfer activity, suggesting cooperative allosteric interactions between RING and G2BR binding. The situation is different in the case of uncharged Ube2G2, which binds the E3 with lower affinity due to loss of some G2BR contacts, an effect that promotes dissociation of reacted (or inactive) E2 from the E3, allowing for exchange with active E2-Ub conjugate
additional information
E2 structure-function analysis, overview. Ube2G2 has a short about 12 amino acid insertion proximal to the E2 active site that determines specificity. In the case of Ube2G2, binding of a non-RING region (G2BR) of its E3, gp78, to the backside of the UBC domain alters the acidic loop conformation, which is helical in the free E2 structure but is unwound in the G2BR-bound structure. The unwinding generates a series of interactions among E2, E3, and Ub that help stabilize a closed E2-Ub conformation to increase aminolysis reactivity. The requirement of an extra, allosteric interaction between Ube2G2 and gp78 ensures that the K48 chain-building E2 cannot work with any RING E3 it happens to contact. The human ERAD E3 ligase, gp78, uses the non-RING G2BR to interact with the backside of its E2, Ube2G2. G2BR binding in trans can increase the affinity of Ube2G2-Ub for the gp78 RING and can enhance both E3-dependent and E3-independent Ub transfer activity, suggesting cooperative allosteric interactions between RING and G2BR binding. The situation is different in the case of uncharged Ube2G2, which binds the E3 with lower affinity due to loss of some G2BR contacts, an effect that promotes dissociation of reacted (or inactive) E2 from the E3, allowing for exchange with active E2-Ub conjugate
additional information
E2 structure-function analysis, overview. Ube2G2 has a short about 12 amino acid insertion proximal to the E2 active site that determines specificity. In the case of Ube2G2, binding of a non-RING region (G2BR) of its E3, gp78, to the backside of the UBC domain alters the acidic loop conformation, which is helical in the free E2 structure but is unwound in the G2BR-bound structure. The unwinding generates a series of interactions among E2, E3, and Ub that help stabilize a closed E2-Ub conformation to increase aminolysis reactivity. The requirement of an extra, allosteric interaction between Ube2G2 and gp78 ensures that the K48 chain-building E2 cannot work with any RING E3 it happens to contact. The human ERAD E3 ligase, gp78, uses the non-RING G2BR to interact with the backside of its E2, Ube2G2. G2BR binding in trans can increase the affinity of Ube2G2-Ub for the gp78 RING and can enhance both E3-dependent and E3-independent Ub transfer activity, suggesting cooperative allosteric interactions between RING and G2BR binding. The situation is different in the case of uncharged Ube2G2, which binds the E3 with lower affinity due to loss of some G2BR contacts, an effect that promotes dissociation of reacted (or inactive) E2 from the E3, allowing for exchange with active E2-Ub conjugate
additional information
E2 structure-function analysis, overview. Ube2G2 has a short about 12 amino acid insertion proximal to the E2 active site that determines specificity. In the case of Ube2G2, binding of a non-RING region (G2BR) of its E3, gp78, to the backside of the UBC domain alters the acidic loop conformation, which is helical in the free E2 structure but is unwound in the G2BR-bound structure. The unwinding generates a series of interactions among E2, E3, and Ub that help stabilize a closed E2-Ub conformation to increase aminolysis reactivity. The requirement of an extra, allosteric interaction between Ube2G2 and gp78 ensures that the K48 chain-building E2 cannot work with any RING E3 it happens to contact. The human ERAD E3 ligase, gp78, uses the non-RING G2BR to interact with the backside of its E2, Ube2G2. G2BR binding in trans can increase the affinity of Ube2G2-Ub for the gp78 RING and can enhance both E3-dependent and E3-independent Ub transfer activity, suggesting cooperative allosteric interactions between RING and G2BR binding. The situation is different in the case of uncharged Ube2G2, which binds the E3 with lower affinity due to loss of some G2BR contacts, an effect that promotes dissociation of reacted (or inactive) E2 from the E3, allowing for exchange with active E2-Ub conjugate
additional information
E2 structure-function analysis, overview. Ube2G2 has a short about 12 amino acid insertion proximal to the E2 active site that determines specificity. In the case of Ube2G2, binding of a non-RING region (G2BR) of its E3, gp78, to the backside of the UBC domain alters the acidic loop conformation, which is helical in the free E2 structure but is unwound in the G2BR-bound structure. The unwinding generates a series of interactions among E2, E3, and Ub that help stabilize a closed E2-Ub conformation to increase aminolysis reactivity. The requirement of an extra, allosteric interaction between Ube2G2 and gp78 ensures that the K48 chain-building E2 cannot work with any RING E3 it happens to contact. The human ERAD E3 ligase, gp78, uses the non-RING G2BR to interact with the backside of its E2, Ube2G2. G2BR binding in trans can increase the affinity of Ube2G2-Ub for the gp78 RING and can enhance both E3-dependent and E3-independent Ub transfer activity, suggesting cooperative allosteric interactions between RING and G2BR binding. The situation is different in the case of uncharged Ube2G2, which binds the E3 with lower affinity due to loss of some G2BR contacts, an effect that promotes dissociation of reacted (or inactive) E2 from the E3, allowing for exchange with active E2-Ub conjugate
additional information
E2 structure-function analysis, overview. Ube2G2 has a short about 12 amino acid insertion proximal to the E2 active site that determines specificity. In the case of Ube2G2, binding of a non-RING region (G2BR) of its E3, gp78, to the backside of the UBC domain alters the acidic loop conformation, which is helical in the free E2 structure but is unwound in the G2BR-bound structure. The unwinding generates a series of interactions among E2, E3, and Ub that help stabilize a closed E2-Ub conformation to increase aminolysis reactivity. The requirement of an extra, allosteric interaction between Ube2G2 and gp78 ensures that the K48 chain-building E2 cannot work with any RING E3 it happens to contact. The human ERAD E3 ligase, gp78, uses the non-RING G2BR to interact with the backside of its E2, Ube2G2. G2BR binding in trans can increase the affinity of Ube2G2-Ub for the gp78 RING and can enhance both E3-dependent and E3-independent Ub transfer activity, suggesting cooperative allosteric interactions between RING and G2BR binding. The situation is different in the case of uncharged Ube2G2, which binds the E3 with lower affinity due to loss of some G2BR contacts, an effect that promotes dissociation of reacted (or inactive) E2 from the E3, allowing for exchange with active E2-Ub conjugate
additional information
E2 structure-function analysis, overview. Ube2G2 has a short about 12 amino acid insertion proximal to the E2 active site that determines specificity. In the case of Ube2G2, binding of a non-RING region (G2BR) of its E3, gp78, to the backside of the UBC domain alters the acidic loop conformation, which is helical in the free E2 structure but is unwound in the G2BR-bound structure. The unwinding generates a series of interactions among E2, E3, and Ub that help stabilize a closed E2-Ub conformation to increase aminolysis reactivity. The requirement of an extra, allosteric interaction between Ube2G2 and gp78 ensures that the K48 chain-building E2 cannot work with any RING E3 it happens to contact. The human ERAD E3 ligase, gp78, uses the non-RING G2BR to interact with the backside of its E2, Ube2G2. G2BR binding in trans can increase the affinity of Ube2G2-Ub for the gp78 RING and can enhance both E3-dependent and E3-independent Ub transfer activity, suggesting cooperative allosteric interactions between RING and G2BR binding. The situation is different in the case of uncharged Ube2G2, which binds the E3 with lower affinity due to loss of some G2BR contacts, an effect that promotes dissociation of reacted (or inactive) E2 from the E3, allowing for exchange with active E2-Ub conjugate
additional information
E2 structure-function analysis, overview. Ube2G2 has a short about 12 amino acid insertion proximal to the E2 active site that determines specificity. In the case of Ube2G2, binding of a non-RING region (G2BR) of its E3, gp78, to the backside of the UBC domain alters the acidic loop conformation, which is helical in the free E2 structure but is unwound in the G2BR-bound structure. The unwinding generates a series of interactions among E2, E3, and Ub that help stabilize a closed E2-Ub conformation to increase aminolysis reactivity. The requirement of an extra, allosteric interaction between Ube2G2 and gp78 ensures that the K48 chain-building E2 cannot work with any RING E3 it happens to contact. The human ERAD E3 ligase, gp78, uses the non-RING G2BR to interact with the backside of its E2, Ube2G2. G2BR binding in trans can increase the affinity of Ube2G2-Ub for the gp78 RING and can enhance both E3-dependent and E3-independent Ub transfer activity, suggesting cooperative allosteric interactions between RING and G2BR binding. The situation is different in the case of uncharged Ube2G2, which binds the E3 with lower affinity due to loss of some G2BR contacts, an effect that promotes dissociation of reacted (or inactive) E2 from the E3, allowing for exchange with active E2-Ub conjugate
additional information
E2 structure-function analysis, overview. Ube2G2 has a short about 12 amino acid insertion proximal to the E2 active site that determines specificity. In the case of Ube2G2, binding of a non-RING region (G2BR) of its E3, gp78, to the backside of the UBC domain alters the acidic loop conformation, which is helical in the free E2 structure but is unwound in the G2BR-bound structure. The unwinding generates a series of interactions among E2, E3, and Ub that help stabilize a closed E2-Ub conformation to increase aminolysis reactivity. The requirement of an extra, allosteric interaction between Ube2G2 and gp78 ensures that the K48 chain-building E2 cannot work with any RING E3 it happens to contact. The human ERAD E3 ligase, gp78, uses the non-RING G2BR to interact with the backside of its E2, Ube2G2. G2BR binding in trans can increase the affinity of Ube2G2-Ub for the gp78 RING and can enhance both E3-dependent and E3-independent Ub transfer activity, suggesting cooperative allosteric interactions between RING and G2BR binding. The situation is different in the case of uncharged Ube2G2, which binds the E3 with lower affinity due to loss of some G2BR contacts, an effect that promotes dissociation of reacted (or inactive) E2 from the E3, allowing for exchange with active E2-Ub conjugate
additional information
E2 structure-function analysis, overview. Ube2G2 has a short about 12 amino acid insertion proximal to the E2 active site that determines specificity. In the case of Ube2G2, binding of a non-RING region (G2BR) of its E3, gp78, to the backside of the UBC domain alters the acidic loop conformation, which is helical in the free E2 structure but is unwound in the G2BR-bound structure. The unwinding generates a series of interactions among E2, E3, and Ub that help stabilize a closed E2-Ub conformation to increase aminolysis reactivity. The requirement of an extra, allosteric interaction between Ube2G2 and gp78 ensures that the K48 chain-building E2 cannot work with any RING E3 it happens to contact. The human ERAD E3 ligase, gp78, uses the non-RING G2BR to interact with the backside of its E2, Ube2G2. G2BR binding in trans can increase the affinity of Ube2G2-Ub for the gp78 RING and can enhance both E3-dependent and E3-independent Ub transfer activity, suggesting cooperative allosteric interactions between RING and G2BR binding. The situation is different in the case of uncharged Ube2G2, which binds the E3 with lower affinity due to loss of some G2BR contacts, an effect that promotes dissociation of reacted (or inactive) E2 from the E3, allowing for exchange with active E2-Ub conjugate
additional information
E2 structure-function analysis, overview. Ube2G2 has a short about 12 amino acid insertion proximal to the E2 active site that determines specificity. In the case of Ube2G2, binding of a non-RING region (G2BR) of its E3, gp78, to the backside of the UBC domain alters the acidic loop conformation, which is helical in the free E2 structure but is unwound in the G2BR-bound structure. The unwinding generates a series of interactions among E2, E3, and Ub that help stabilize a closed E2-Ub conformation to increase aminolysis reactivity. The requirement of an extra, allosteric interaction between Ube2G2 and gp78 ensures that the K48 chain-building E2 cannot work with any RING E3 it happens to contact. The human ERAD E3 ligase, gp78, uses the non-RING G2BR to interact with the backside of its E2, Ube2G2. G2BR binding in trans can increase the affinity of Ube2G2-Ub for the gp78 RING and can enhance both E3-dependent and E3-independent Ub transfer activity, suggesting cooperative allosteric interactions between RING and G2BR binding. The situation is different in the case of uncharged Ube2G2, which binds the E3 with lower affinity due to loss of some G2BR contacts, an effect that promotes dissociation of reacted (or inactive) E2 from the E3, allowing for exchange with active E2-Ub conjugate
additional information
E2 structure-function analysis, overview. Ube2G2 has a short about 12 amino acid insertion proximal to the E2 active site that determines specificity. In the case of Ube2G2, binding of a non-RING region (G2BR) of its E3, gp78, to the backside of the UBC domain alters the acidic loop conformation, which is helical in the free E2 structure but is unwound in the G2BR-bound structure. The unwinding generates a series of interactions among E2, E3, and Ub that help stabilize a closed E2-Ub conformation to increase aminolysis reactivity. The requirement of an extra, allosteric interaction between Ube2G2 and gp78 ensures that the K48 chain-building E2 cannot work with any RING E3 it happens to contact. The human ERAD E3 ligase, gp78, uses the non-RING G2BR to interact with the backside of its E2, Ube2G2. G2BR binding in trans can increase the affinity of Ube2G2-Ub for the gp78 RING and can enhance both E3-dependent and E3-independent Ub transfer activity, suggesting cooperative allosteric interactions between RING and G2BR binding. The situation is different in the case of uncharged Ube2G2, which binds the E3 with lower affinity due to loss of some G2BR contacts, an effect that promotes dissociation of reacted (or inactive) E2 from the E3, allowing for exchange with active E2-Ub conjugate
additional information
E2 structure-function analysis, overview. Ube2G2 has a short about 12 amino acid insertion proximal to the E2 active site that determines specificity. In the case of Ube2G2, binding of a non-RING region (G2BR) of its E3, gp78, to the backside of the UBC domain alters the acidic loop conformation, which is helical in the free E2 structure but is unwound in the G2BR-bound structure. The unwinding generates a series of interactions among E2, E3, and Ub that help stabilize a closed E2-Ub conformation to increase aminolysis reactivity. The requirement of an extra, allosteric interaction between Ube2G2 and gp78 ensures that the K48 chain-building E2 cannot work with any RING E3 it happens to contact. The human ERAD E3 ligase, gp78, uses the non-RING G2BR to interact with the backside of its E2, Ube2G2. G2BR binding in trans can increase the affinity of Ube2G2-Ub for the gp78 RING and can enhance both E3-dependent and E3-independent Ub transfer activity, suggesting cooperative allosteric interactions between RING and G2BR binding. The situation is different in the case of uncharged Ube2G2, which binds the E3 with lower affinity due to loss of some G2BR contacts, an effect that promotes dissociation of reacted (or inactive) E2 from the E3, allowing for exchange with active E2-Ub conjugate
additional information
E2 structure-function analysis, overview. Ube2G2 has a short about 12 amino acid insertion proximal to the E2 active site that determines specificity. In the case of Ube2G2, binding of a non-RING region (G2BR) of its E3, gp78, to the backside of the UBC domain alters the acidic loop conformation, which is helical in the free E2 structure but is unwound in the G2BR-bound structure. The unwinding generates a series of interactions among E2, E3, and Ub that help stabilize a closed E2-Ub conformation to increase aminolysis reactivity. The requirement of an extra, allosteric interaction between Ube2G2 and gp78 ensures that the K48 chain-building E2 cannot work with any RING E3 it happens to contact. The human ERAD E3 ligase, gp78, uses the non-RING G2BR to interact with the backside of its E2, Ube2G2. G2BR binding in trans can increase the affinity of Ube2G2-Ub for the gp78 RING and can enhance both E3-dependent and E3-independent Ub transfer activity, suggesting cooperative allosteric interactions between RING and G2BR binding. The situation is different in the case of uncharged Ube2G2, which binds the E3 with lower affinity due to loss of some G2BR contacts, an effect that promotes dissociation of reacted (or inactive) E2 from the E3, allowing for exchange with active E2-Ub conjugate
additional information
E2 structure-function analysis, overview. Ube2G2 has a short about 12 amino acid insertion proximal to the E2 active site that determines specificity. In the case of Ube2G2, binding of a non-RING region (G2BR) of its E3, gp78, to the backside of the UBC domain alters the acidic loop conformation, which is helical in the free E2 structure but is unwound in the G2BR-bound structure. The unwinding generates a series of interactions among E2, E3, and Ub that help stabilize a closed E2-Ub conformation to increase aminolysis reactivity. The requirement of an extra, allosteric interaction between Ube2G2 and gp78 ensures that the K48 chain-building E2 cannot work with any RING E3 it happens to contact. The human ERAD E3 ligase, gp78, uses the non-RING G2BR to interact with the backside of its E2, Ube2G2. G2BR binding in trans can increase the affinity of Ube2G2-Ub for the gp78 RING and can enhance both E3-dependent and E3-independent Ub transfer activity, suggesting cooperative allosteric interactions between RING and G2BR binding. The situation is different in the case of uncharged Ube2G2, which binds the E3 with lower affinity due to loss of some G2BR contacts, an effect that promotes dissociation of reacted (or inactive) E2 from the E3, allowing for exchange with active E2-Ub conjugate
additional information
E2 structure-function analysis, overview. Ube2G2 has a short about 12 amino acid insertion proximal to the E2 active site that determines specificity. In the case of Ube2G2, binding of a non-RING region (G2BR) of its E3, gp78, to the backside of the UBC domain alters the acidic loop conformation, which is helical in the free E2 structure but is unwound in the G2BR-bound structure. The unwinding generates a series of interactions among E2, E3, and Ub that help stabilize a closed E2-Ub conformation to increase aminolysis reactivity. The requirement of an extra, allosteric interaction between Ube2G2 and gp78 ensures that the K48 chain-building E2 cannot work with any RING E3 it happens to contact. The human ERAD E3 ligase, gp78, uses the non-RING G2BR to interact with the backside of its E2, Ube2G2. G2BR binding in trans can increase the affinity of Ube2G2-Ub for the gp78 RING and can enhance both E3-dependent and E3-independent Ub transfer activity, suggesting cooperative allosteric interactions between RING and G2BR binding. The situation is different in the case of uncharged Ube2G2, which binds the E3 with lower affinity due to loss of some G2BR contacts, an effect that promotes dissociation of reacted (or inactive) E2 from the E3, allowing for exchange with active E2-Ub conjugate
additional information
E2 structure-function analysis, overview. Ube2G2 has a short about 12 amino acid insertion proximal to the E2 active site that determines specificity. In the case of Ube2G2, binding of a non-RING region (G2BR) of its E3, gp78, to the backside of the UBC domain alters the acidic loop conformation, which is helical in the free E2 structure but is unwound in the G2BR-bound structure. The unwinding generates a series of interactions among E2, E3, and Ub that help stabilize a closed E2-Ub conformation to increase aminolysis reactivity. The requirement of an extra, allosteric interaction between Ube2G2 and gp78 ensures that the K48 chain-building E2 cannot work with any RING E3 it happens to contact. The human ERAD E3 ligase, gp78, uses the non-RING G2BR to interact with the backside of its E2, Ube2G2. G2BR binding in trans can increase the affinity of Ube2G2-Ub for the gp78 RING and can enhance both E3-dependent and E3-independent Ub transfer activity, suggesting cooperative allosteric interactions between RING and G2BR binding. The situation is different in the case of uncharged Ube2G2, which binds the E3 with lower affinity due to loss of some G2BR contacts, an effect that promotes dissociation of reacted (or inactive) E2 from the E3, allowing for exchange with active E2-Ub conjugate
additional information
E2 structure-function analysis, overview. Ube2G2 has a short about 12 amino acid insertion proximal to the E2 active site that determines specificity. In the case of Ube2G2, binding of a non-RING region (G2BR) of its E3, gp78, to the backside of the UBC domain alters the acidic loop conformation, which is helical in the free E2 structure but is unwound in the G2BR-bound structure. The unwinding generates a series of interactions among E2, E3, and Ub that help stabilize a closed E2-Ub conformation to increase aminolysis reactivity. The requirement of an extra, allosteric interaction between Ube2G2 and gp78 ensures that the K48 chain-building E2 cannot work with any RING E3 it happens to contact. The human ERAD E3 ligase, gp78, uses the non-RING G2BR to interact with the backside of its E2, Ube2G2. G2BR binding in trans can increase the affinity of Ube2G2-Ub for the gp78 RING and can enhance both E3-dependent and E3-independent Ub transfer activity, suggesting cooperative allosteric interactions between RING and G2BR binding. The situation is different in the case of uncharged Ube2G2, which binds the E3 with lower affinity due to loss of some G2BR contacts, an effect that promotes dissociation of reacted (or inactive) E2 from the E3, allowing for exchange with active E2-Ub conjugate
additional information
E2 structure-function analysis, overview. Ube2G2 has a short about 12 amino acid insertion proximal to the E2 active site that determines specificity. In the case of Ube2G2, binding of a non-RING region (G2BR) of its E3, gp78, to the backside of the UBC domain alters the acidic loop conformation, which is helical in the free E2 structure but is unwound in the G2BR-bound structure. The unwinding generates a series of interactions among E2, E3, and Ub that help stabilize a closed E2-Ub conformation to increase aminolysis reactivity. The requirement of an extra, allosteric interaction between Ube2G2 and gp78 ensures that the K48 chain-building E2 cannot work with any RING E3 it happens to contact. The human ERAD E3 ligase, gp78, uses the non-RING G2BR to interact with the backside of its E2, Ube2G2. G2BR binding in trans can increase the affinity of Ube2G2-Ub for the gp78 RING and can enhance both E3-dependent and E3-independent Ub transfer activity, suggesting cooperative allosteric interactions between RING and G2BR binding. The situation is different in the case of uncharged Ube2G2, which binds the E3 with lower affinity due to loss of some G2BR contacts, an effect that promotes dissociation of reacted (or inactive) E2 from the E3, allowing for exchange with active E2-Ub conjugate
additional information
E2 structure-function analysis, overview. Ube2G2 has a short about 12 amino acid insertion proximal to the E2 active site that determines specificity. In the case of Ube2G2, binding of a non-RING region (G2BR) of its E3, gp78, to the backside of the UBC domain alters the acidic loop conformation, which is helical in the free E2 structure but is unwound in the G2BR-bound structure. The unwinding generates a series of interactions among E2, E3, and Ub that help stabilize a closed E2-Ub conformation to increase aminolysis reactivity. The requirement of an extra, allosteric interaction between Ube2G2 and gp78 ensures that the K48 chain-building E2 cannot work with any RING E3 it happens to contact. The human ERAD E3 ligase, gp78, uses the non-RING G2BR to interact with the backside of its E2, Ube2G2. G2BR binding in trans can increase the affinity of Ube2G2-Ub for the gp78 RING and can enhance both E3-dependent and E3-independent Ub transfer activity, suggesting cooperative allosteric interactions between RING and G2BR binding. The situation is different in the case of uncharged Ube2G2, which binds the E3 with lower affinity due to loss of some G2BR contacts, an effect that promotes dissociation of reacted (or inactive) E2 from the E3, allowing for exchange with active E2-Ub conjugate
additional information
E2 structure-function analysis, overview. Ube2G2 has a short about 12 amino acid insertion proximal to the E2 active site that determines specificity. In the case of Ube2G2, binding of a non-RING region (G2BR) of its E3, gp78, to the backside of the UBC domain alters the acidic loop conformation, which is helical in the free E2 structure but is unwound in the G2BR-bound structure. The unwinding generates a series of interactions among E2, E3, and Ub that help stabilize a closed E2-Ub conformation to increase aminolysis reactivity. The requirement of an extra, allosteric interaction between Ube2G2 and gp78 ensures that the K48 chain-building E2 cannot work with any RING E3 it happens to contact. The human ERAD E3 ligase, gp78, uses the non-RING G2BR to interact with the backside of its E2, Ube2G2. G2BR binding in trans can increase the affinity of Ube2G2-Ub for the gp78 RING and can enhance both E3-dependent and E3-independent Ub transfer activity, suggesting cooperative allosteric interactions between RING and G2BR binding. The situation is different in the case of uncharged Ube2G2, which binds the E3 with lower affinity due to loss of some G2BR contacts, an effect that promotes dissociation of reacted (or inactive) E2 from the E3, allowing for exchange with active E2-Ub conjugate
additional information
E2 structure-function analysis, overview. Ube2G2 has a short about 12 amino acid insertion proximal to the E2 active site that determines specificity. In the case of Ube2G2, binding of a non-RING region (G2BR) of its E3, gp78, to the backside of the UBC domain alters the acidic loop conformation, which is helical in the free E2 structure but is unwound in the G2BR-bound structure. The unwinding generates a series of interactions among E2, E3, and Ub that help stabilize a closed E2-Ub conformation to increase aminolysis reactivity. The requirement of an extra, allosteric interaction between Ube2G2 and gp78 ensures that the K48 chain-building E2 cannot work with any RING E3 it happens to contact. The human ERAD E3 ligase, gp78, uses the non-RING G2BR to interact with the backside of its E2, Ube2G2. G2BR binding in trans can increase the affinity of Ube2G2-Ub for the gp78 RING and can enhance both E3-dependent and E3-independent Ub transfer activity, suggesting cooperative allosteric interactions between RING and G2BR binding. The situation is different in the case of uncharged Ube2G2, which binds the E3 with lower affinity due to loss of some G2BR contacts, an effect that promotes dissociation of reacted (or inactive) E2 from the E3, allowing for exchange with active E2-Ub conjugate
additional information
E2 structure-function analysis, overview. Ube2G2 has a short about 12 amino acid insertion proximal to the E2 active site that determines specificity. In the case of Ube2G2, binding of a non-RING region (G2BR) of its E3, gp78, to the backside of the UBC domain alters the acidic loop conformation, which is helical in the free E2 structure but is unwound in the G2BR-bound structure. The unwinding generates a series of interactions among E2, E3, and Ub that help stabilize a closed E2-Ub conformation to increase aminolysis reactivity. The requirement of an extra, allosteric interaction between Ube2G2 and gp78 ensures that the K48 chain-building E2 cannot work with any RING E3 it happens to contact. The human ERAD E3 ligase, gp78, uses the non-RING G2BR to interact with the backside of its E2, Ube2G2. G2BR binding in trans can increase the affinity of Ube2G2-Ub for the gp78 RING and can enhance both E3-dependent and E3-independent Ub transfer activity, suggesting cooperative allosteric interactions between RING and G2BR binding. The situation is different in the case of uncharged Ube2G2, which binds the E3 with lower affinity due to loss of some G2BR contacts, an effect that promotes dissociation of reacted (or inactive) E2 from the E3, allowing for exchange with active E2-Ub conjugate
additional information
E2 structure-function analysis, overview. Ube2G2 has a short about 12 amino acid insertion proximal to the E2 active site that determines specificity. In the case of Ube2G2, binding of a non-RING region (G2BR) of its E3, gp78, to the backside of the UBC domain alters the acidic loop conformation, which is helical in the free E2 structure but is unwound in the G2BR-bound structure. The unwinding generates a series of interactions among E2, E3, and Ub that help stabilize a closed E2-Ub conformation to increase aminolysis reactivity. The requirement of an extra, allosteric interaction between Ube2G2 and gp78 ensures that the K48 chain-building E2 cannot work with any RING E3 it happens to contact. The human ERAD E3 ligase, gp78, uses the non-RING G2BR to interact with the backside of its E2, Ube2G2. G2BR binding in trans can increase the affinity of Ube2G2-Ub for the gp78 RING and can enhance both E3-dependent and E3-independent Ub transfer activity, suggesting cooperative allosteric interactions between RING and G2BR binding. The situation is different in the case of uncharged Ube2G2, which binds the E3 with lower affinity due to loss of some G2BR contacts, an effect that promotes dissociation of reacted (or inactive) E2 from the E3, allowing for exchange with active E2-Ub conjugate
additional information
E2 structure-function analysis, overview. Ube2G2 has a short about 12 amino acid insertion proximal to the E2 active site that determines specificity. In the case of Ube2G2, binding of a non-RING region (G2BR) of its E3, gp78, to the backside of the UBC domain alters the acidic loop conformation, which is helical in the free E2 structure but is unwound in the G2BR-bound structure. The unwinding generates a series of interactions among E2, E3, and Ub that help stabilize a closed E2-Ub conformation to increase aminolysis reactivity. The requirement of an extra, allosteric interaction between Ube2G2 and gp78 ensures that the K48 chain-building E2 cannot work with any RING E3 it happens to contact. The human ERAD E3 ligase, gp78, uses the non-RING G2BR to interact with the backside of its E2, Ube2G2. G2BR binding in trans can increase the affinity of Ube2G2-Ub for the gp78 RING and can enhance both E3-dependent and E3-independent Ub transfer activity, suggesting cooperative allosteric interactions between RING and G2BR binding. The situation is different in the case of uncharged Ube2G2, which binds the E3 with lower affinity due to loss of some G2BR contacts, an effect that promotes dissociation of reacted (or inactive) E2 from the E3, allowing for exchange with active E2-Ub conjugate
additional information
E2 structure-function analysis, overview. Ube2N-Ub conjugates show an array of orientations that involve little or no contact between the E2 and ubiquitin (open states) and some conformations (closed states) that involve contacts between the Ub hydrophobic patch centered on Ub I44 and residues in the E2 crossover helix. Although the Ube2N-Ub conjugates is highly dynamic, the ensembles of conformations adopted by it are different in terms of the relative fraction of closed versus open states
additional information
E2 structure-function analysis, overview. Ube2N-Ub conjugates show an array of orientations that involve little or no contact between the E2 and ubiquitin (open states) and some conformations (closed states) that involve contacts between the Ub hydrophobic patch centered on Ub I44 and residues in the E2 crossover helix. Although the Ube2N-Ub conjugates is highly dynamic, the ensembles of conformations adopted by it are different in terms of the relative fraction of closed versus open states
additional information
E2 structure-function analysis, overview. Ube2N-Ub conjugates show an array of orientations that involve little or no contact between the E2 and ubiquitin (open states) and some conformations (closed states) that involve contacts between the Ub hydrophobic patch centered on Ub I44 and residues in the E2 crossover helix. Although the Ube2N-Ub conjugates is highly dynamic, the ensembles of conformations adopted by it are different in terms of the relative fraction of closed versus open states
additional information
E2 structure-function analysis, overview. Ube2N-Ub conjugates show an array of orientations that involve little or no contact between the E2 and ubiquitin (open states) and some conformations (closed states) that involve contacts between the Ub hydrophobic patch centered on Ub I44 and residues in the E2 crossover helix. Although the Ube2N-Ub conjugates is highly dynamic, the ensembles of conformations adopted by it are different in terms of the relative fraction of closed versus open states
additional information
E2 structure-function analysis, overview. Ube2N-Ub conjugates show an array of orientations that involve little or no contact between the E2 and ubiquitin (open states) and some conformations (closed states) that involve contacts between the Ub hydrophobic patch centered on Ub I44 and residues in the E2 crossover helix. Although the Ube2N-Ub conjugates is highly dynamic, the ensembles of conformations adopted by it are different in terms of the relative fraction of closed versus open states
additional information
E2 structure-function analysis, overview. Ube2N-Ub conjugates show an array of orientations that involve little or no contact between the E2 and ubiquitin (open states) and some conformations (closed states) that involve contacts between the Ub hydrophobic patch centered on Ub I44 and residues in the E2 crossover helix. Although the Ube2N-Ub conjugates is highly dynamic, the ensembles of conformations adopted by it are different in terms of the relative fraction of closed versus open states
additional information
E2 structure-function analysis, overview. Ube2N-Ub conjugates show an array of orientations that involve little or no contact between the E2 and ubiquitin (open states) and some conformations (closed states) that involve contacts between the Ub hydrophobic patch centered on Ub I44 and residues in the E2 crossover helix. Although the Ube2N-Ub conjugates is highly dynamic, the ensembles of conformations adopted by it are different in terms of the relative fraction of closed versus open states
additional information
E2 structure-function analysis, overview. Ube2N-Ub conjugates show an array of orientations that involve little or no contact between the E2 and ubiquitin (open states) and some conformations (closed states) that involve contacts between the Ub hydrophobic patch centered on Ub I44 and residues in the E2 crossover helix. Although the Ube2N-Ub conjugates is highly dynamic, the ensembles of conformations adopted by it are different in terms of the relative fraction of closed versus open states
additional information
E2 structure-function analysis, overview. Ube2N-Ub conjugates show an array of orientations that involve little or no contact between the E2 and ubiquitin (open states) and some conformations (closed states) that involve contacts between the Ub hydrophobic patch centered on Ub I44 and residues in the E2 crossover helix. Although the Ube2N-Ub conjugates is highly dynamic, the ensembles of conformations adopted by it are different in terms of the relative fraction of closed versus open states
additional information
E2 structure-function analysis, overview. Ube2N-Ub conjugates show an array of orientations that involve little or no contact between the E2 and ubiquitin (open states) and some conformations (closed states) that involve contacts between the Ub hydrophobic patch centered on Ub I44 and residues in the E2 crossover helix. Although the Ube2N-Ub conjugates is highly dynamic, the ensembles of conformations adopted by it are different in terms of the relative fraction of closed versus open states
additional information
E2 structure-function analysis, overview. Ube2N-Ub conjugates show an array of orientations that involve little or no contact between the E2 and ubiquitin (open states) and some conformations (closed states) that involve contacts between the Ub hydrophobic patch centered on Ub I44 and residues in the E2 crossover helix. Although the Ube2N-Ub conjugates is highly dynamic, the ensembles of conformations adopted by it are different in terms of the relative fraction of closed versus open states
additional information
E2 structure-function analysis, overview. Ube2N-Ub conjugates show an array of orientations that involve little or no contact between the E2 and ubiquitin (open states) and some conformations (closed states) that involve contacts between the Ub hydrophobic patch centered on Ub I44 and residues in the E2 crossover helix. Although the Ube2N-Ub conjugates is highly dynamic, the ensembles of conformations adopted by it are different in terms of the relative fraction of closed versus open states
additional information
E2 structure-function analysis, overview. Ube2N-Ub conjugates show an array of orientations that involve little or no contact between the E2 and ubiquitin (open states) and some conformations (closed states) that involve contacts between the Ub hydrophobic patch centered on Ub I44 and residues in the E2 crossover helix. Although the Ube2N-Ub conjugates is highly dynamic, the ensembles of conformations adopted by it are different in terms of the relative fraction of closed versus open states
additional information
E2 structure-function analysis, overview. Ube2N-Ub conjugates show an array of orientations that involve little or no contact between the E2 and ubiquitin (open states) and some conformations (closed states) that involve contacts between the Ub hydrophobic patch centered on Ub I44 and residues in the E2 crossover helix. Although the Ube2N-Ub conjugates is highly dynamic, the ensembles of conformations adopted by it are different in terms of the relative fraction of closed versus open states
additional information
E2 structure-function analysis, overview. Ube2N-Ub conjugates show an array of orientations that involve little or no contact between the E2 and ubiquitin (open states) and some conformations (closed states) that involve contacts between the Ub hydrophobic patch centered on Ub I44 and residues in the E2 crossover helix. Although the Ube2N-Ub conjugates is highly dynamic, the ensembles of conformations adopted by it are different in terms of the relative fraction of closed versus open states
additional information
E2 structure-function analysis, overview. Ube2N-Ub conjugates show an array of orientations that involve little or no contact between the E2 and ubiquitin (open states) and some conformations (closed states) that involve contacts between the Ub hydrophobic patch centered on Ub I44 and residues in the E2 crossover helix. Although the Ube2N-Ub conjugates is highly dynamic, the ensembles of conformations adopted by it are different in terms of the relative fraction of closed versus open states
additional information
E2 structure-function analysis, overview. Ube2N-Ub conjugates show an array of orientations that involve little or no contact between the E2 and ubiquitin (open states) and some conformations (closed states) that involve contacts between the Ub hydrophobic patch centered on Ub I44 and residues in the E2 crossover helix. Although the Ube2N-Ub conjugates is highly dynamic, the ensembles of conformations adopted by it are different in terms of the relative fraction of closed versus open states
additional information
E2 structure-function analysis, overview. Ube2N-Ub conjugates show an array of orientations that involve little or no contact between the E2 and ubiquitin (open states) and some conformations (closed states) that involve contacts between the Ub hydrophobic patch centered on Ub I44 and residues in the E2 crossover helix. Although the Ube2N-Ub conjugates is highly dynamic, the ensembles of conformations adopted by it are different in terms of the relative fraction of closed versus open states
additional information
E2 structure-function analysis, overview. Ube2N-Ub conjugates show an array of orientations that involve little or no contact between the E2 and ubiquitin (open states) and some conformations (closed states) that involve contacts between the Ub hydrophobic patch centered on Ub I44 and residues in the E2 crossover helix. Although the Ube2N-Ub conjugates is highly dynamic, the ensembles of conformations adopted by it are different in terms of the relative fraction of closed versus open states
additional information
E2 structure-function analysis, overview. Ube2N-Ub conjugates show an array of orientations that involve little or no contact between the E2 and ubiquitin (open states) and some conformations (closed states) that involve contacts between the Ub hydrophobic patch centered on Ub I44 and residues in the E2 crossover helix. Although the Ube2N-Ub conjugates is highly dynamic, the ensembles of conformations adopted by it are different in terms of the relative fraction of closed versus open states
additional information
E2 structure-function analysis, overview. Ube2N-Ub conjugates show an array of orientations that involve little or no contact between the E2 and ubiquitin (open states) and some conformations (closed states) that involve contacts between the Ub hydrophobic patch centered on Ub I44 and residues in the E2 crossover helix. Although the Ube2N-Ub conjugates is highly dynamic, the ensembles of conformations adopted by it are different in terms of the relative fraction of closed versus open states
additional information
E2 structure-function analysis, overview. Ube2N-Ub conjugates show an array of orientations that involve little or no contact between the E2 and ubiquitin (open states) and some conformations (closed states) that involve contacts between the Ub hydrophobic patch centered on Ub I44 and residues in the E2 crossover helix. Although the Ube2N-Ub conjugates is highly dynamic, the ensembles of conformations adopted by it are different in terms of the relative fraction of closed versus open states
additional information
E2 structure-function analysis, overview. Ube2N-Ub conjugates show an array of orientations that involve little or no contact between the E2 and ubiquitin (open states) and some conformations (closed states) that involve contacts between the Ub hydrophobic patch centered on Ub I44 and residues in the E2 crossover helix. Although the Ube2N-Ub conjugates is highly dynamic, the ensembles of conformations adopted by it are different in terms of the relative fraction of closed versus open states
additional information
E2 structure-function analysis, overview. Ube2N-Ub conjugates show an array of orientations that involve little or no contact between the E2 and ubiquitin (open states) and some conformations (closed states) that involve contacts between the Ub hydrophobic patch centered on Ub I44 and residues in the E2 crossover helix. Although the Ube2N-Ub conjugates is highly dynamic, the ensembles of conformations adopted by it are different in terms of the relative fraction of closed versus open states
additional information
E2 structure-function analysis, overview. Ube2N-Ub conjugates show an array of orientations that involve little or no contact between the E2 and ubiquitin (open states) and some conformations (closed states) that involve contacts between the Ub hydrophobic patch centered on Ub I44 and residues in the E2 crossover helix. Although the Ube2N-Ub conjugates is highly dynamic, the ensembles of conformations adopted by it are different in terms of the relative fraction of closed versus open states
additional information
E2 structure-function analysis, overview. Ube2N-Ub conjugates show an array of orientations that involve little or no contact between the E2 and ubiquitin (open states) and some conformations (closed states) that involve contacts between the Ub hydrophobic patch centered on Ub I44 and residues in the E2 crossover helix. Although the Ube2N-Ub conjugates is highly dynamic, the ensembles of conformations adopted by it are different in terms of the relative fraction of closed versus open states
additional information
E2 structure-function analysis, overview. Ube2N-Ub conjugates show an array of orientations that involve little or no contact between the E2 and ubiquitin (open states) and some conformations (closed states) that involve contacts between the Ub hydrophobic patch centered on Ub I44 and residues in the E2 crossover helix. Although the Ube2N-Ub conjugates is highly dynamic, the ensembles of conformations adopted by it are different in terms of the relative fraction of closed versus open states
additional information
E2 structure-function analysis, overview. Ube2N-Ub conjugates show an array of orientations that involve little or no contact between the E2 and ubiquitin (open states) and some conformations (closed states) that involve contacts between the Ub hydrophobic patch centered on Ub I44 and residues in the E2 crossover helix. Although the Ube2N-Ub conjugates is highly dynamic, the ensembles of conformations adopted by it are different in terms of the relative fraction of closed versus open states
additional information
E2 structure-function analysis, overview. Ube2N-Ub conjugates show an array of orientations that involve little or no contact between the E2 and ubiquitin (open states) and some conformations (closed states) that involve contacts between the Ub hydrophobic patch centered on Ub I44 and residues in the E2 crossover helix. Although the Ube2N-Ub conjugates is highly dynamic, the ensembles of conformations adopted by it are different in terms of the relative fraction of closed versus open states
additional information
E2 structure-function analysis, overview. Ube2N-Ub conjugates show an array of orientations that involve little or no contact between the E2 and ubiquitin (open states) and some conformations (closed states) that involve contacts between the Ub hydrophobic patch centered on Ub I44 and residues in the E2 crossover helix. Although the Ube2N-Ub conjugates is highly dynamic, the ensembles of conformations adopted by it are different in terms of the relative fraction of closed versus open states
additional information
E2 structure-function analysis, overview. Ube2S uses acidic residues in the final UBC domain helix to interact with the acceptor Ub and orient K11 towards the C-terminus of the donor Ub bound to its active site
additional information
E2 structure-function analysis, overview. Ube2S uses acidic residues in the final UBC domain helix to interact with the acceptor Ub and orient K11 towards the C-terminus of the donor Ub bound to its active site
additional information
E2 structure-function analysis, overview. Ube2S uses acidic residues in the final UBC domain helix to interact with the acceptor Ub and orient K11 towards the C-terminus of the donor Ub bound to its active site
additional information
E2 structure-function analysis, overview. Ube2S uses acidic residues in the final UBC domain helix to interact with the acceptor Ub and orient K11 towards the C-terminus of the donor Ub bound to its active site
additional information
E2 structure-function analysis, overview. Ube2S uses acidic residues in the final UBC domain helix to interact with the acceptor Ub and orient K11 towards the C-terminus of the donor Ub bound to its active site
additional information
E2 structure-function analysis, overview. Ube2S uses acidic residues in the final UBC domain helix to interact with the acceptor Ub and orient K11 towards the C-terminus of the donor Ub bound to its active site
additional information
E2 structure-function analysis, overview. Ube2S uses acidic residues in the final UBC domain helix to interact with the acceptor Ub and orient K11 towards the C-terminus of the donor Ub bound to its active site
additional information
E2 structure-function analysis, overview. Ube2S uses acidic residues in the final UBC domain helix to interact with the acceptor Ub and orient K11 towards the C-terminus of the donor Ub bound to its active site
additional information
E2 structure-function analysis, overview. Ube2S uses acidic residues in the final UBC domain helix to interact with the acceptor Ub and orient K11 towards the C-terminus of the donor Ub bound to its active site
additional information
E2 structure-function analysis, overview. Ube2S uses acidic residues in the final UBC domain helix to interact with the acceptor Ub and orient K11 towards the C-terminus of the donor Ub bound to its active site
additional information
E2 structure-function analysis, overview. Ube2S uses acidic residues in the final UBC domain helix to interact with the acceptor Ub and orient K11 towards the C-terminus of the donor Ub bound to its active site
additional information
E2 structure-function analysis, overview. Ube2S uses acidic residues in the final UBC domain helix to interact with the acceptor Ub and orient K11 towards the C-terminus of the donor Ub bound to its active site
additional information
E2 structure-function analysis, overview. Ube2S uses acidic residues in the final UBC domain helix to interact with the acceptor Ub and orient K11 towards the C-terminus of the donor Ub bound to its active site
additional information
E2 structure-function analysis, overview. Ube2S uses acidic residues in the final UBC domain helix to interact with the acceptor Ub and orient K11 towards the C-terminus of the donor Ub bound to its active site
additional information
E2 structure-function analysis, overview. Ube2S uses acidic residues in the final UBC domain helix to interact with the acceptor Ub and orient K11 towards the C-terminus of the donor Ub bound to its active site
additional information
E2 structure-function analysis, overview. Ube2S uses acidic residues in the final UBC domain helix to interact with the acceptor Ub and orient K11 towards the C-terminus of the donor Ub bound to its active site
additional information
E2 structure-function analysis, overview. Ube2S uses acidic residues in the final UBC domain helix to interact with the acceptor Ub and orient K11 towards the C-terminus of the donor Ub bound to its active site
additional information
E2 structure-function analysis, overview. Ube2S uses acidic residues in the final UBC domain helix to interact with the acceptor Ub and orient K11 towards the C-terminus of the donor Ub bound to its active site
additional information
E2 structure-function analysis, overview. Ube2S uses acidic residues in the final UBC domain helix to interact with the acceptor Ub and orient K11 towards the C-terminus of the donor Ub bound to its active site
additional information
E2 structure-function analysis, overview. Ube2S uses acidic residues in the final UBC domain helix to interact with the acceptor Ub and orient K11 towards the C-terminus of the donor Ub bound to its active site
additional information
E2 structure-function analysis, overview. Ube2S uses acidic residues in the final UBC domain helix to interact with the acceptor Ub and orient K11 towards the C-terminus of the donor Ub bound to its active site
additional information
E2 structure-function analysis, overview. Ube2S uses acidic residues in the final UBC domain helix to interact with the acceptor Ub and orient K11 towards the C-terminus of the donor Ub bound to its active site
additional information
E2 structure-function analysis, overview. Ube2S uses acidic residues in the final UBC domain helix to interact with the acceptor Ub and orient K11 towards the C-terminus of the donor Ub bound to its active site
additional information
E2 structure-function analysis, overview. Ube2S uses acidic residues in the final UBC domain helix to interact with the acceptor Ub and orient K11 towards the C-terminus of the donor Ub bound to its active site
additional information
E2 structure-function analysis, overview. Ube2S uses acidic residues in the final UBC domain helix to interact with the acceptor Ub and orient K11 towards the C-terminus of the donor Ub bound to its active site
additional information
E2 structure-function analysis, overview. Ube2S uses acidic residues in the final UBC domain helix to interact with the acceptor Ub and orient K11 towards the C-terminus of the donor Ub bound to its active site
additional information
E2 structure-function analysis, overview. Ube2S uses acidic residues in the final UBC domain helix to interact with the acceptor Ub and orient K11 towards the C-terminus of the donor Ub bound to its active site
additional information
E2 structure-function analysis, overview. Ube2S uses acidic residues in the final UBC domain helix to interact with the acceptor Ub and orient K11 towards the C-terminus of the donor Ub bound to its active site
additional information
E2 structure-function analysis, overview. Ube2S uses acidic residues in the final UBC domain helix to interact with the acceptor Ub and orient K11 towards the C-terminus of the donor Ub bound to its active site
additional information
E2 structure-function analysis, overview. Ube2S uses acidic residues in the final UBC domain helix to interact with the acceptor Ub and orient K11 towards the C-terminus of the donor Ub bound to its active site
additional information
the structure of UBE2Z enzyme provides functional insight into specificity in the FAT10 protein conjugation machinery. UBE2Z is specific for E1-like ubiquitin-activating enzyme UBA6. UBE2Z N-terminal extension and loop LB are essential for selectivity toward UBA6
additional information
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analyis of the molecular basis by which Cdc34 engages its E1, and the structural mechanisms, by which its unique C-terminal extension functions in Cdc34 activity. Conformational changes in Uba1 and Cdc34 and a unique binding mode are required for transthiolation. The Cdc34-Ub structure reveals contacts between the Cdc34 C-terminal extension and Ub that stabilize Cdc34-Ub in a closed conformation and are critical for Ub discharge
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Show AA Sequence and Transmembrane Helices (3914 entries)
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PDB
SCOP
CATH
UNIPROT
ORGANISM
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MOLECULAR WEIGHT
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
18000
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2 * 18000, single band on SDS-PAGE, indicating a dimeric form. Gel filtration results in an estimated molecular weight of 42 kDa
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SUBUNIT
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
dimer
additional information
dimer
-
2 * 18000, single band on SDS-PAGE, indicating a dimeric form. Gel filtration results in an estimated molecular weight of 42 kDa
dimer
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E2 enzymes spontaneously dimerize in solution, in vitro, in absence of charged ubiquitin
additional information
UBE2J1 shows the UBC + insert-Ext domain organization
additional information
UBE2J1 shows the UBC + insert-Ext domain organization
additional information
UBE2J1 shows the UBC + insert-Ext domain organization
additional information
UBE2J1 shows the UBC + insert-Ext domain organization
additional information
UBE2J1 shows the UBC + insert-Ext domain organization
additional information
UBE2J1 shows the UBC + insert-Ext domain organization
additional information
UBE2J1 shows the UBC + insert-Ext domain organization
additional information
UBE2J1 shows the UBC + insert-Ext domain organization
additional information
UBE2J1 shows the UBC + insert-Ext domain organization
additional information
UBE2J1 shows the UBC + insert-Ext domain organization
additional information
UBE2J1 shows the UBC + insert-Ext domain organization
additional information
UBE2J1 shows the UBC + insert-Ext domain organization
additional information
UBE2J1 shows the UBC + insert-Ext domain organization
additional information
UBE2J1 shows the UBC + insert-Ext domain organization
additional information
UBE2J1 shows the UBC + insert-Ext domain organization
additional information
UBE2J1 shows the UBC + insert-Ext domain organization
additional information
UBE2J1 shows the UBC + insert-Ext domain organization
additional information
UBE2J1 shows the UBC + insert-Ext domain organization
additional information
UBE2J1 shows the UBC + insert-Ext domain organization
additional information
UBE2J1 shows the UBC + insert-Ext domain organization
additional information
UBE2J1 shows the UBC + insert-Ext domain organization
additional information
UBE2J1 shows the UBC + insert-Ext domain organization
additional information
UBE2J1 shows the UBC + insert-Ext domain organization
additional information
UBE2J1 shows the UBC + insert-Ext domain organization
additional information
UBE2J1 shows the UBC + insert-Ext domain organization
additional information
UBE2J1 shows the UBC + insert-Ext domain organization
additional information
UBE2J1 shows the UBC + insert-Ext domain organization
additional information
UBE2J1 shows the UBC + insert-Ext domain organization
additional information
UBE2J1 shows the UBC + insert-Ext domain organization
additional information
UBE2J1 shows the UBC + insert-Ext domain organization
additional information
UBE2J2 shows the UBC + insert-Ext domain organization
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UBE2J2 shows the UBC + insert-Ext domain organization
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UBE2J2 shows the UBC + insert-Ext domain organization
additional information
UBE2J2 shows the UBC + insert-Ext domain organization
additional information
UBE2J2 shows the UBC + insert-Ext domain organization
additional information
UBE2J2 shows the UBC + insert-Ext domain organization
additional information
UBE2J2 shows the UBC + insert-Ext domain organization
additional information
UBE2J2 shows the UBC + insert-Ext domain organization
additional information
UBE2J2 shows the UBC + insert-Ext domain organization
additional information
UBE2J2 shows the UBC + insert-Ext domain organization
additional information
UBE2J2 shows the UBC + insert-Ext domain organization
additional information
UBE2J2 shows the UBC + insert-Ext domain organization
additional information
UBE2J2 shows the UBC + insert-Ext domain organization
additional information
UBE2J2 shows the UBC + insert-Ext domain organization
additional information
UBE2J2 shows the UBC + insert-Ext domain organization
additional information
UBE2J2 shows the UBC + insert-Ext domain organization
additional information
UBE2J2 shows the UBC + insert-Ext domain organization
additional information
UBE2J2 shows the UBC + insert-Ext domain organization
additional information
UBE2J2 shows the UBC + insert-Ext domain organization
additional information
UBE2J2 shows the UBC + insert-Ext domain organization
additional information
UBE2J2 shows the UBC + insert-Ext domain organization
additional information
UBE2J2 shows the UBC + insert-Ext domain organization
additional information
UBE2J2 shows the UBC + insert-Ext domain organization
additional information
UBE2J2 shows the UBC + insert-Ext domain organization
additional information
UBE2J2 shows the UBC + insert-Ext domain organization
additional information
UBE2J2 shows the UBC + insert-Ext domain organization
additional information
UBE2J2 shows the UBC + insert-Ext domain organization
additional information
UBE2J2 shows the UBC + insert-Ext domain organization
additional information
UBE2J2 shows the UBC + insert-Ext domain organization
additional information
UBE2J2 shows the UBC + insert-Ext domain organization
additional information
UBE2K shows the UBC-UBA domain organization, an additional structured domain is linked to their UBC domain. Ube2K has a unique region near its active site that interacts with a tyrosine near K48 in the acceptor Ub to provide K48-linkage specificity
additional information
UBE2K shows the UBC-UBA domain organization, an additional structured domain is linked to their UBC domain. Ube2K has a unique region near its active site that interacts with a tyrosine near K48 in the acceptor Ub to provide K48-linkage specificity
additional information
UBE2K shows the UBC-UBA domain organization, an additional structured domain is linked to their UBC domain. Ube2K has a unique region near its active site that interacts with a tyrosine near K48 in the acceptor Ub to provide K48-linkage specificity
additional information
UBE2K shows the UBC-UBA domain organization, an additional structured domain is linked to their UBC domain. Ube2K has a unique region near its active site that interacts with a tyrosine near K48 in the acceptor Ub to provide K48-linkage specificity
additional information
UBE2K shows the UBC-UBA domain organization, an additional structured domain is linked to their UBC domain. Ube2K has a unique region near its active site that interacts with a tyrosine near K48 in the acceptor Ub to provide K48-linkage specificity
additional information
UBE2K shows the UBC-UBA domain organization, an additional structured domain is linked to their UBC domain. Ube2K has a unique region near its active site that interacts with a tyrosine near K48 in the acceptor Ub to provide K48-linkage specificity
additional information
UBE2K shows the UBC-UBA domain organization, an additional structured domain is linked to their UBC domain. Ube2K has a unique region near its active site that interacts with a tyrosine near K48 in the acceptor Ub to provide K48-linkage specificity
additional information
UBE2K shows the UBC-UBA domain organization, an additional structured domain is linked to their UBC domain. Ube2K has a unique region near its active site that interacts with a tyrosine near K48 in the acceptor Ub to provide K48-linkage specificity
additional information
UBE2K shows the UBC-UBA domain organization, an additional structured domain is linked to their UBC domain. Ube2K has a unique region near its active site that interacts with a tyrosine near K48 in the acceptor Ub to provide K48-linkage specificity
additional information
UBE2K shows the UBC-UBA domain organization, an additional structured domain is linked to their UBC domain. Ube2K has a unique region near its active site that interacts with a tyrosine near K48 in the acceptor Ub to provide K48-linkage specificity
additional information
UBE2K shows the UBC-UBA domain organization, an additional structured domain is linked to their UBC domain. Ube2K has a unique region near its active site that interacts with a tyrosine near K48 in the acceptor Ub to provide K48-linkage specificity
additional information
UBE2K shows the UBC-UBA domain organization, an additional structured domain is linked to their UBC domain. Ube2K has a unique region near its active site that interacts with a tyrosine near K48 in the acceptor Ub to provide K48-linkage specificity
additional information
UBE2K shows the UBC-UBA domain organization, an additional structured domain is linked to their UBC domain. Ube2K has a unique region near its active site that interacts with a tyrosine near K48 in the acceptor Ub to provide K48-linkage specificity
additional information
UBE2K shows the UBC-UBA domain organization, an additional structured domain is linked to their UBC domain. Ube2K has a unique region near its active site that interacts with a tyrosine near K48 in the acceptor Ub to provide K48-linkage specificity
additional information
UBE2K shows the UBC-UBA domain organization, an additional structured domain is linked to their UBC domain. Ube2K has a unique region near its active site that interacts with a tyrosine near K48 in the acceptor Ub to provide K48-linkage specificity
additional information
UBE2K shows the UBC-UBA domain organization, an additional structured domain is linked to their UBC domain. Ube2K has a unique region near its active site that interacts with a tyrosine near K48 in the acceptor Ub to provide K48-linkage specificity
additional information
UBE2K shows the UBC-UBA domain organization, an additional structured domain is linked to their UBC domain. Ube2K has a unique region near its active site that interacts with a tyrosine near K48 in the acceptor Ub to provide K48-linkage specificity
additional information
UBE2K shows the UBC-UBA domain organization, an additional structured domain is linked to their UBC domain. Ube2K has a unique region near its active site that interacts with a tyrosine near K48 in the acceptor Ub to provide K48-linkage specificity
additional information
UBE2K shows the UBC-UBA domain organization, an additional structured domain is linked to their UBC domain. Ube2K has a unique region near its active site that interacts with a tyrosine near K48 in the acceptor Ub to provide K48-linkage specificity
additional information
UBE2K shows the UBC-UBA domain organization, an additional structured domain is linked to their UBC domain. Ube2K has a unique region near its active site that interacts with a tyrosine near K48 in the acceptor Ub to provide K48-linkage specificity
additional information
UBE2K shows the UBC-UBA domain organization, an additional structured domain is linked to their UBC domain. Ube2K has a unique region near its active site that interacts with a tyrosine near K48 in the acceptor Ub to provide K48-linkage specificity
additional information
UBE2K shows the UBC-UBA domain organization, an additional structured domain is linked to their UBC domain. Ube2K has a unique region near its active site that interacts with a tyrosine near K48 in the acceptor Ub to provide K48-linkage specificity
additional information
UBE2K shows the UBC-UBA domain organization, an additional structured domain is linked to their UBC domain. Ube2K has a unique region near its active site that interacts with a tyrosine near K48 in the acceptor Ub to provide K48-linkage specificity
additional information
UBE2K shows the UBC-UBA domain organization, an additional structured domain is linked to their UBC domain. Ube2K has a unique region near its active site that interacts with a tyrosine near K48 in the acceptor Ub to provide K48-linkage specificity
additional information
UBE2K shows the UBC-UBA domain organization, an additional structured domain is linked to their UBC domain. Ube2K has a unique region near its active site that interacts with a tyrosine near K48 in the acceptor Ub to provide K48-linkage specificity
additional information
UBE2K shows the UBC-UBA domain organization, an additional structured domain is linked to their UBC domain. Ube2K has a unique region near its active site that interacts with a tyrosine near K48 in the acceptor Ub to provide K48-linkage specificity
additional information
UBE2K shows the UBC-UBA domain organization, an additional structured domain is linked to their UBC domain. Ube2K has a unique region near its active site that interacts with a tyrosine near K48 in the acceptor Ub to provide K48-linkage specificity
additional information
UBE2K shows the UBC-UBA domain organization, an additional structured domain is linked to their UBC domain. Ube2K has a unique region near its active site that interacts with a tyrosine near K48 in the acceptor Ub to provide K48-linkage specificity
additional information
UBE2K shows the UBC-UBA domain organization, an additional structured domain is linked to their UBC domain. Ube2K has a unique region near its active site that interacts with a tyrosine near K48 in the acceptor Ub to provide K48-linkage specificity
additional information
UBE2K shows the UBC-UBA domain organization, an additional structured domain is linked to their UBC domain. Ube2K has a unique region near its active site that interacts with a tyrosine near K48 in the acceptor Ub to provide K48-linkage specificity
additional information
UBE2Q1 shows the Ext-UBC + insert domain organization
additional information
UBE2Q1 shows the Ext-UBC + insert domain organization
additional information
UBE2Q1 shows the Ext-UBC + insert domain organization
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UBE2Q1 shows the Ext-UBC + insert domain organization
additional information
UBE2Q1 shows the Ext-UBC + insert domain organization
additional information
UBE2Q1 shows the Ext-UBC + insert domain organization
additional information
UBE2Q1 shows the Ext-UBC + insert domain organization
additional information
UBE2Q1 shows the Ext-UBC + insert domain organization
additional information
UBE2Q1 shows the Ext-UBC + insert domain organization
additional information
UBE2Q1 shows the Ext-UBC + insert domain organization
additional information
UBE2Q1 shows the Ext-UBC + insert domain organization
additional information
UBE2Q1 shows the Ext-UBC + insert domain organization
additional information
UBE2Q1 shows the Ext-UBC + insert domain organization
additional information
UBE2Q1 shows the Ext-UBC + insert domain organization
additional information
UBE2Q1 shows the Ext-UBC + insert domain organization
additional information
UBE2Q1 shows the Ext-UBC + insert domain organization
additional information
UBE2Q1 shows the Ext-UBC + insert domain organization
additional information
UBE2Q1 shows the Ext-UBC + insert domain organization
additional information
UBE2Q1 shows the Ext-UBC + insert domain organization
additional information
UBE2Q1 shows the Ext-UBC + insert domain organization
additional information
UBE2Q1 shows the Ext-UBC + insert domain organization
additional information
UBE2Q1 shows the Ext-UBC + insert domain organization
additional information
UBE2Q1 shows the Ext-UBC + insert domain organization
additional information
UBE2Q1 shows the Ext-UBC + insert domain organization
additional information
UBE2Q1 shows the Ext-UBC + insert domain organization
additional information
UBE2Q1 shows the Ext-UBC + insert domain organization
additional information
UBE2Q1 shows the Ext-UBC + insert domain organization
additional information
UBE2Q1 shows the Ext-UBC + insert domain organization
additional information
UBE2Q1 shows the Ext-UBC + insert domain organization
additional information
UBE2Q1 shows the Ext-UBC + insert domain organization
additional information
UBE2R1 shows the UBC + insert-Ext domain organization
additional information
UBE2R1 shows the UBC + insert-Ext domain organization
additional information
UBE2R1 shows the UBC + insert-Ext domain organization
additional information
UBE2R1 shows the UBC + insert-Ext domain organization
additional information
UBE2R1 shows the UBC + insert-Ext domain organization
additional information
UBE2R1 shows the UBC + insert-Ext domain organization
additional information
UBE2R1 shows the UBC + insert-Ext domain organization
additional information
UBE2R1 shows the UBC + insert-Ext domain organization
additional information
UBE2R1 shows the UBC + insert-Ext domain organization
additional information
UBE2R1 shows the UBC + insert-Ext domain organization
additional information
UBE2R1 shows the UBC + insert-Ext domain organization
additional information
UBE2R1 shows the UBC + insert-Ext domain organization
additional information
UBE2R1 shows the UBC + insert-Ext domain organization
additional information
UBE2R1 shows the UBC + insert-Ext domain organization
additional information
UBE2R1 shows the UBC + insert-Ext domain organization
additional information
UBE2R1 shows the UBC + insert-Ext domain organization
additional information
UBE2R1 shows the UBC + insert-Ext domain organization
additional information
UBE2R1 shows the UBC + insert-Ext domain organization
additional information
UBE2R1 shows the UBC + insert-Ext domain organization
additional information
UBE2R1 shows the UBC + insert-Ext domain organization
additional information
UBE2R1 shows the UBC + insert-Ext domain organization
additional information
UBE2R1 shows the UBC + insert-Ext domain organization
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UBE2R1 shows the UBC + insert-Ext domain organization
additional information
UBE2R1 shows the UBC + insert-Ext domain organization
additional information
UBE2R1 shows the UBC + insert-Ext domain organization
additional information
UBE2R1 shows the UBC + insert-Ext domain organization
additional information
UBE2R1 shows the UBC + insert-Ext domain organization
additional information
UBE2R1 shows the UBC + insert-Ext domain organization
additional information
UBE2R1 shows the UBC + insert-Ext domain organization
additional information
UBE2R1 shows the UBC + insert-Ext domain organization
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UBE2R2 shows the UBC + insert-Ext domain organization
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UBE2R2 shows the UBC + insert-Ext domain organization
additional information
UBE2R2 shows the UBC + insert-Ext domain organization
additional information
UBE2R2 shows the UBC + insert-Ext domain organization
additional information
UBE2R2 shows the UBC + insert-Ext domain organization
additional information
UBE2R2 shows the UBC + insert-Ext domain organization
additional information
UBE2R2 shows the UBC + insert-Ext domain organization
additional information
UBE2R2 shows the UBC + insert-Ext domain organization
additional information
UBE2R2 shows the UBC + insert-Ext domain organization
additional information
UBE2R2 shows the UBC + insert-Ext domain organization
additional information
UBE2R2 shows the UBC + insert-Ext domain organization
additional information
UBE2R2 shows the UBC + insert-Ext domain organization
additional information
UBE2R2 shows the UBC + insert-Ext domain organization
additional information
UBE2R2 shows the UBC + insert-Ext domain organization
additional information
UBE2R2 shows the UBC + insert-Ext domain organization
additional information
UBE2R2 shows the UBC + insert-Ext domain organization
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UBE2R2 shows the UBC + insert-Ext domain organization
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UBE2R2 shows the UBC + insert-Ext domain organization
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UBE2R2 shows the UBC + insert-Ext domain organization
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UBE2R2 shows the UBC + insert-Ext domain organization
additional information
UBE2R2 shows the UBC + insert-Ext domain organization
additional information
UBE2R2 shows the UBC + insert-Ext domain organization
additional information
UBE2R2 shows the UBC + insert-Ext domain organization
additional information
UBE2R2 shows the UBC + insert-Ext domain organization
additional information
UBE2R2 shows the UBC + insert-Ext domain organization
additional information
UBE2R2 shows the UBC + insert-Ext domain organization
additional information
UBE2R2 shows the UBC + insert-Ext domain organization
additional information
UBE2R2 shows the UBC + insert-Ext domain organization
additional information
UBE2R2 shows the UBC + insert-Ext domain organization
additional information
UBE2R2 shows the UBC + insert-Ext domain organization
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UBE2Z is a 354-residue-long atypical ubiquitin conjugating enzyme comprising about 100-residue long N- and C-terminal extensions on top of the conserved core UBC domain, classifying it as a class IV E2 enzyme. The UBE2Z core domain adopts the characteristic ellipsoid shape of UBC domains but also harbors two extensions termed loops LA (residues 169-173) and LB (residues 194-197) compared with the prototypical class I E2 enzyme UBE2D3. Structural organization of UBE2Z, modeling, overview
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UBC6e exists in at least two different configurations: as an apparent monomer and as part of a complex
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isoformUbc2 interacts with disease-related protein SGT1
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POSTTRANSLATIONAL MODIFICATION
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
sumoylation
additional information
sumoylation
conjugation of the small ubiquitin-like modifier (SUMO) to protein substrates is an important disease-associated posttranslational modification. The E2 enzyme Ubc9 is sumoylated
sumoylation
A1L167, O00762, O14933, P49427, P49459, P51668, P51965, P60604, P61077, P61086, P61088, P62253, P62256, P62837, P63146, P68036, Q13404, Q15819, Q16763, Q5JXB2, Q5VVX9, Q712K3, Q7Z7E8, Q8N2K1, Q8WVN8, Q969T4, Q96LR5, Q9H832, Q9NPD8, Q9Y385
SUMO modification of an E2 occurs on the polyUb chain-building E2, Ube2K. Like Ube2I, the site of modification is on helix alpha1, but on a residue in the E1 and E3 binding interface, consistent with the decreased activity observed in vitro
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ubiquitination is involved in myriad cell and disease pathways. The ubiquitin-conjugating E2 is the central player in the ubiquitin-transfer pathway
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isoform Pex4 can form a disulfide bond between the cysteine residues at positions 105 and 146. Mutating the disulfide forming cysteine residues to serines does not disturb the secondary structure of the protein but does reduce the in vitro activity of Pex4. Structure of mutant C105S/C146S in complex with the soluble domain of peroxisomal membrane protein Pex22 shows a narrowing of the active site cleft, caused by loss of the disulfide bond. This modification of the active site microenvironment is likely to restrict access of ubiquitin to the active site cysteine, modulating Pex4 activity
additional information
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isoform Pex4 can form a disulfide bond between the cysteine residues at positions 105 and 146. Mutating the disulfide forming cysteine residues to serines does not disturb the secondary structure of the protein but does reduce the in vitro activity of Pex4. Structure of mutant C105S/C146S in complex with the soluble domain of peroxisomal membrane protein Pex22 shows a narrowing of the active site cleft, caused by loss of the disulfide bond. This modification of the active site microenvironment is likely to restrict access of ubiquitin to the active site cysteine, modulating Pex4 activity
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CRYSTALLIZATION (Commentary)
ORGANISM
UNIPROT
LITERATURE
recombinant enzyme, N-terminally His-tagged, subcloned in Escherichia coli BL21(DE2), via pET28 vector, purified using Ni-NTA column and HiLoad 16/60 Superdex 75 gel filtration column, diffracted X-rays to 1.7 A. The crystal belongs to space group C2
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using 20% (w/v) PEG 3350, 0.2 M sodium acetate, and 0.1 M Bis-Tris, pH 6.5
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2.9 A crystal structure of the ubiquitin ligase CHIP U-box domain complexed with UbcH5a. CHIP binds to UbcH5 and Ubc13 through similar specificity determinants located on the long loops and central helix of the CHIP U-box, and on the N-terminal helix and loops L4 and L7 of its cognate E2 enzymes including a key S-P-A motif. The determinants make different relative contributions to the overall interactions between CHIP and the two E2 enzymes. CHIP undergoes auto-ubiquitination by UbcH5
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
Cdc34 alone and in complex with E1, and a Cdc34-Ub thioester mimetic representing the product of Uba1-Cdc34 Ub transthiolation, sitting drop method, mixing of 200 nl of 8.7 mg/ml Uba1-Cdc34DELTAdist crosslink and 0.116 mM Ub, 1 mM ATP, and 5 mM MgCl2, with 200 nl of mother liquor containing 0.2 M ammonium sulfate, 25% PEG 3,350, 0.1 M Bis-Tris, pH 6.5, 18°C, for the free Cdc34DELTAdist, hanging drop method is used with 10 mg/ml protein and mother liquor containing 0.06 M zinc acetate, 0.108 M sodium cacodylate, 14.4% PEG 8000, and 20% glycerol, 18°C, a 1.3fold excess of Cdc34 inhibitor CC0651 is used as a crystallization aid, X-ray diffraction structure determination and analysis at 1.65-2.07 A resolution, molecular replacement using structure PDB ID 3CMM as the search model, modeling
crystal structures of the C-terminal ubiquitin fold domain from yeast Uba2 alone and in complex with E2 enzyme Ubc9. Uba2 undergoes remarkable conformational changes during the reaction. The structure of the Uba2 domain-Ubc9 complex reveals interactions unique to Sumo E1 and E2. Comparison with a previous Ubc9-E3 complex structure demonstrates overlap between Uba2 and E3 binding sites on Ubc9, indicating that loading with Sumo and E3-catalyzed transfer to substrates are strictly separate steps
mutant C105S/C146S in complex with the soluble domain of peroxisomal membrane protein Pex22. Structure shows a narrowing of the active site cleft, caused by loss of the disulfide bond
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PROTEIN VARIANTS
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
A157C
a naturally occuring mutation involved in the Fanconi anaemia syndrome
C136F
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mutation results in constitutive binding of UbcM2 to transcription factor Nrf2 and an increased half-life of the transcription factor in vivo
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
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
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
C105S/C146S
mutation of the residues forming an intramolecular disulfide bond. Mutation does not disturb the secondary structure of the protein but does reduce the in vitro activity of isoform Pex4
K118R
residue Lys118 is required for Ubc7 activity. Mutant is very poor in assembly of polyubiquitin chains. Lys118 is both essential and sufficient for Doa10-mediated degradation of substrates
P93L
additional information
P93L
temperature-sensitive mutant in which cell cycle progression is arrested at mitosis. The mutant grows normally at the restrictive temperature when spindle assembly checkpoint is inactivated, suggesting that the arrest is not due to abnormal spindle assembly, but rather due to prolonged activation of spindle assembly checkpoint
P93L
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temperature-sensitive mutant in which cell cycle progression is arrested at mitosis. The mutant grows normally at the restrictive temperature when spindle assembly checkpoint is inactivated, suggesting that the arrest is not due to abnormal spindle assembly, but rather due to prolonged activation of spindle assembly checkpoint
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additional information
DNA damage-induced foci of E2 ubiquitin-conjugating enzyme are detectable upon co-transfection with an interacting E3 ubiquitin ligase
additional information
DNA damage-induced foci of E2 ubiquitin-conjugating enzyme are detectable upon co-transfection with an interacting E3 ubiquitin ligase
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enzyme knockout by UBE2J2 siRNA in Hep-G2 cells. HEK293T cells lacking the E2 ubiquitin-conjugating enzymes UBE2J1, UBE2J2, and UBE2G2 are generated using a limited CRISPR/Cas9-based library. Hap1 cells lacking UBE2J2 are generated by CRISPR/Cas9-mediated genome editing
additional information
enzyme knockout by UBE2J2 siRNA in Hep-G2 cells. HEK293T cells lacking the E2 ubiquitin-conjugating enzymes UBE2J1, UBE2J2, and UBE2G2 are generated using a limited CRISPR/Cas9-based library. Hap1 cells lacking UBE2J2 are generated by CRISPR/Cas9-mediated genome editing
additional information
enzyme knockout by UBE2J2 siRNA in Hep-G2 cells. HEK293T cells lacking the E2 ubiquitin-conjugating enzymes UBE2J1, UBE2J2, and UBE2G2 are generated using a limited CRISPR/Cas9-based library. Hap1 cells lacking UBE2J2 are generated by CRISPR/Cas9-mediated genome editing
additional information
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enzyme knockout by UBE2J2 siRNA in Hep-G2 cells. HEK293T cells lacking the E2 ubiquitin-conjugating enzymes UBE2J1, UBE2J2, and UBE2G2 are generated using a limited CRISPR/Cas9-based library. Hap1 cells lacking UBE2J2 are generated by CRISPR/Cas9-mediated genome editing
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enzyme UBE2B knockout, HONE-1 and TW01 cells are transfected specific UBE2B siRNA
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enzyme UBE2B knockout, HONE-1 and TW01 cells are transfected specific UBE2B siRNA
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generation of deletion mutants UBE2ZDELTALB and UBE2ZDELTANter
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genome analysis for patient PNGS-252 revealed a maternal c.4C>G missense alteration resulting in the Gln2Glu amino acid substitution and a paternal 23 kb deletion across the UBE2T locus. The Gln2 residue in helix1 of UBE2T is not an integral part of the UBE2T-FANCL interaction surface
additional information
genome analysis for patient PNGS-252 revealed a maternal c.4C>G missense alteration resulting in the Gln2Glu amino acid substitution and a paternal 23 kb deletion across the UBE2T locus. The Gln2 residue in helix1 of UBE2T is not an integral part of the UBE2T-FANCL interaction surface
additional information
HEK293T cells lacking the E2 ubiquitin-conjugating enzymes UBE2J1, UBE2J2 and UBE2G2 are generated using a limited CRISPR/Cas9-based library
additional information
HEK293T cells lacking the E2 ubiquitin-conjugating enzymes UBE2J1, UBE2J2 and UBE2G2 are generated using a limited CRISPR/Cas9-based library
additional information
HEK293T cells lacking the E2 ubiquitin-conjugating enzymes UBE2J1, UBE2J2 and UBE2G2 are generated using a limited CRISPR/Cas9-based library
additional information
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HEK293T cells lacking the E2 ubiquitin-conjugating enzymes UBE2J1, UBE2J2 and UBE2G2 are generated using a limited CRISPR/Cas9-based library
additional information
HEK293T cells lacking the E2 ubiquitin-conjugating enzymes UBE2J1, UBE2J2, and UBE2G2 are generated using a limited CRISPR/Cas9-based library
additional information
HEK293T cells lacking the E2 ubiquitin-conjugating enzymes UBE2J1, UBE2J2, and UBE2G2 are generated using a limited CRISPR/Cas9-based library
additional information
HEK293T cells lacking the E2 ubiquitin-conjugating enzymes UBE2J1, UBE2J2, and UBE2G2 are generated using a limited CRISPR/Cas9-based library
additional information
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HEK293T cells lacking the E2 ubiquitin-conjugating enzymes UBE2J1, UBE2J2, and UBE2G2 are generated using a limited CRISPR/Cas9-based library
additional information
knockdown of enzyme UBE2T by specific siRNA in BGC-823 cells and HTB-103 cells can induce G1/S phase arrest in gastric cancer cells, which in turn contributes to the stimulating growth properties of gastric cancer cells. Overexpression of UBE2T in AGS cells and CRL-5974 cells. Phenotypes, overview
additional information
lentiviral CRISPR/Cas9 library targeting of all known human E2 enzymes is used to assess their involvement in US2-mediated HLA-I downregulation. CRISPR gRNAs targeting UBE2D3 induce rescue of eGFP-HLA-A2 expression in US2-expressing cell. The anti-UBE2D3 gRNAs also increase the levels of endogenous HLA-A3 in these US2-expressing cells
additional information
lentiviral CRISPR/Cas9 library targeting of all known human E2 enzymes is used to assess their involvement in US2-mediated HLA-I downregulation. CRISPR gRNAs targeting UBE2D3 induce rescue of eGFP-HLA-A2 expression in US2-expressing cell. The anti-UBE2D3 gRNAs also increase the levels of endogenous HLA-A3 in these US2-expressing cells
additional information
lentiviral CRISPR/Cas9 library targeting of all known human E2 enzymes is used to assess their involvement in US2-mediated HLA-I downregulation. CRISPR gRNAs targeting UBE2D3 induce rescue of eGFP-HLA-A2 expression in US2-expressing cell. The anti-UBE2D3 gRNAs also increase the levels of endogenous HLA-A3 in these US2-expressing cells
additional information
-
lentiviral CRISPR/Cas9 library targeting of all known human E2 enzymes is used to assess their involvement in US2-mediated HLA-I downregulation. CRISPR gRNAs targeting UBE2D3 induce rescue of eGFP-HLA-A2 expression in US2-expressing cell. The anti-UBE2D3 gRNAs also increase the levels of endogenous HLA-A3 in these US2-expressing cells
additional information
lentiviral CRISPR/Cas9 library targeting of all known human E2 enzymes is used to assess their involvement in US2-mediated HLA-I downregulation. Generation of a UBE2G2-null cell line. CRISPR gRNAs targeting UBE2G2 induce rescue of eGFP-HLA-A2 expression in US2-expressing cell. Expression of gRNAs targeting UBE2G2 induce the strongest rescue of eGFP-HLA-A2. The anti-UBE2G2 gRNAs also increase the levels of endogenous HLA-A3 in these US2-expressing cells. By contrast, targeting the UBE2G2 homologue UBE2G1 with CRISPR gRNAs does not affect eGFP-HLA-A2 expressions. Removal of UBE2G2 in causes a growth defect, but is not lethal. HLA-I levels are increased in UBE2G2-null cells compared to control cells, and US2 protein levels are increased, likely due to the stabilization of the US2 ERAD complex in the absence of UBE2G2
additional information
lentiviral CRISPR/Cas9 library targeting of all known human E2 enzymes is used to assess their involvement in US2-mediated HLA-I downregulation. Generation of a UBE2G2-null cell line. CRISPR gRNAs targeting UBE2G2 induce rescue of eGFP-HLA-A2 expression in US2-expressing cell. Expression of gRNAs targeting UBE2G2 induce the strongest rescue of eGFP-HLA-A2. The anti-UBE2G2 gRNAs also increase the levels of endogenous HLA-A3 in these US2-expressing cells. By contrast, targeting the UBE2G2 homologue UBE2G1 with CRISPR gRNAs does not affect eGFP-HLA-A2 expressions. Removal of UBE2G2 in causes a growth defect, but is not lethal. HLA-I levels are increased in UBE2G2-null cells compared to control cells, and US2 protein levels are increased, likely due to the stabilization of the US2 ERAD complex in the absence of UBE2G2
additional information
lentiviral CRISPR/Cas9 library targeting of all known human E2 enzymes is used to assess their involvement in US2-mediated HLA-I downregulation. Generation of a UBE2G2-null cell line. CRISPR gRNAs targeting UBE2G2 induce rescue of eGFP-HLA-A2 expression in US2-expressing cell. Expression of gRNAs targeting UBE2G2 induce the strongest rescue of eGFP-HLA-A2. The anti-UBE2G2 gRNAs also increase the levels of endogenous HLA-A3 in these US2-expressing cells. By contrast, targeting the UBE2G2 homologue UBE2G1 with CRISPR gRNAs does not affect eGFP-HLA-A2 expressions. Removal of UBE2G2 in causes a growth defect, but is not lethal. HLA-I levels are increased in UBE2G2-null cells compared to control cells, and US2 protein levels are increased, likely due to the stabilization of the US2 ERAD complex in the absence of UBE2G2
additional information
-
lentiviral CRISPR/Cas9 library targeting of all known human E2 enzymes is used to assess their involvement in US2-mediated HLA-I downregulation. Generation of a UBE2G2-null cell line. CRISPR gRNAs targeting UBE2G2 induce rescue of eGFP-HLA-A2 expression in US2-expressing cell. Expression of gRNAs targeting UBE2G2 induce the strongest rescue of eGFP-HLA-A2. The anti-UBE2G2 gRNAs also increase the levels of endogenous HLA-A3 in these US2-expressing cells. By contrast, targeting the UBE2G2 homologue UBE2G1 with CRISPR gRNAs does not affect eGFP-HLA-A2 expressions. Removal of UBE2G2 in causes a growth defect, but is not lethal. HLA-I levels are increased in UBE2G2-null cells compared to control cells, and US2 protein levels are increased, likely due to the stabilization of the US2 ERAD complex in the absence of UBE2G2
additional information
lentiviral CRISPR/Cas9 library targeting of all known human E2 enzymes is used to assess their involvement in US2-mediated HLA-I downregulation. Generation of a UBE2J2-null cell line. The strong increase inHLA-I degradation upon UBE2J2 knockout is not caused by increased US2 levels. UBE2J2 depletion increases TRC8 expression levels in the presence of US2, and in this way, enhances US2-mediated HLA-I downregulation
additional information
lentiviral CRISPR/Cas9 library targeting of all known human E2 enzymes is used to assess their involvement in US2-mediated HLA-I downregulation. Generation of a UBE2J2-null cell line. The strong increase inHLA-I degradation upon UBE2J2 knockout is not caused by increased US2 levels. UBE2J2 depletion increases TRC8 expression levels in the presence of US2, and in this way, enhances US2-mediated HLA-I downregulation
additional information
lentiviral CRISPR/Cas9 library targeting of all known human E2 enzymes is used to assess their involvement in US2-mediated HLA-I downregulation. Generation of a UBE2J2-null cell line. The strong increase inHLA-I degradation upon UBE2J2 knockout is not caused by increased US2 levels. UBE2J2 depletion increases TRC8 expression levels in the presence of US2, and in this way, enhances US2-mediated HLA-I downregulation
additional information
-
lentiviral CRISPR/Cas9 library targeting of all known human E2 enzymes is used to assess their involvement in US2-mediated HLA-I downregulation. Generation of a UBE2J2-null cell line. The strong increase inHLA-I degradation upon UBE2J2 knockout is not caused by increased US2 levels. UBE2J2 depletion increases TRC8 expression levels in the presence of US2, and in this way, enhances US2-mediated HLA-I downregulation
additional information
molecular dynamics simulations for E2-25K and the Q126L/D127G active site gate mutants
additional information
Ube2D1 enzyme knockdown by specific shRNA. Treatment of HeLa cells with Ube2D1 shRNA results in a over 90% reduction in Ube2D1 protein and a 3fold increase in March-I expression, as determined by quantitative immunoblot analysis. The increase in March-I protein expression in Ube2D1 knockdown cells is correlated precisely with reduced ubiquitination of March-I
additional information
generation of UbeC6 deletion mice, phenotype, detailed overview. Generation of Derlin2-/- mice showing that not only ERAD enhancers but also UBC6e itself are upregulated
additional information
generation of a Cdc34 active site Cys to Lys mutant
additional information
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generation of a Cdc34 active site Cys to Lys mutant
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PURIFICATION (Commentary)
ORGANISM
UNIPROT
LITERATURE
recombinant enzyme, N-terminally His-tagged, subcloned in Escherichia coli BL21(DE2), via pET28 vector, purified using Ni-NTA column and HiLoad 16/60 Superdex 75 gel filtration column, purity 95% after two steps
-
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 His-tagged enzyme from Escherichia coli strain BL21 (DE3) Codon Plus by nickel affinity chromatography
recombinant His-tagged enzyme from Escherichia coli strain BL21 (DE3) Codon Plus by nickel affinity chromatography
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CLONED (Commentary)
ORGANISM
UNIPROT
LITERATURE
a fragment of the enzyme is cloned into a virus-induced genesilencing vector based on the geminivirus tomato mottlevirus
-
chromosome localization and gene duplication analysis of VvUBCs, phylogenetic analysis, transcriptome analysis, detailed overview
-
expressed and transformed into Escherichia coli (BL-21 DE3) using pET22 vector in frame to a C-terminal His6 tag
-
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, 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)
subcloned in Escherichia coli BL21(DE2), via pET28 vector, N-terminally His-tagged
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gene cdc34, recombinant His-tagged enzyme expression in Escherichia coli strain BL21 (DE3) Codon Plus
gene cdc34, recombinant His-tagged enzyme expression in Escherichia coli strain BL21 (DE3) Codon Plus
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EXPRESSION
ORGANISM
UNIPROT
LITERATURE
expression analysis of response of Vitis vinifera ubiquitin-conjugating enzymes (VvUBCs) to different abiotic stresses, in response to cold and heat, some enzymes are upreguated, while some are downregulated, overview. Salt or water-deficit stress do not cause remarkable changes during 16 days in cv. Cabernet Sauvignon
-
isoform UBC1 mRNA expression is induced by either dehydration, high salinity or by the exogenous abscisic acid
the expression of the enzyme is significantly up-regulated after cold-treatment at 4C lasting for 4, 6, and 8 h
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
the expression of the enzyme is significantly up-regulated after cold-treatment at 4C lasting for 4, 6, and 8 h
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the expression of the enzyme is significantly up-regulated after cold-treatment at 4C lasting for 4, 6, and 8 h
-
-
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APPLICATION
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
diagnostics
ubiquitin-conjugating enzyme E2T is an independent prognostic factor and promotes gastric cancer progression
drug development
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
drug development
-
UbcA1 shows antitumor properties, a potential anticancer drug candidate
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
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REF.
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YEAR
ORGANISM (UNIPROT)
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51
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2012
Mus musculus (Q9Z1K5)
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287
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Homo sapiens (P22314), Homo sapiens (Q8TBC4)
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19
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2000
Homo sapiens (P62837)
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Unver, T.; Turktas, M.; Budak, H.
In planta evidence for the involvement of a ubiquitin conjugating enzyme (UBI E2 Clade) in negative regulation of disease resistance
Plant Mol. Biol. Rep.
31
323-334
2013
Nicotiana benthamiana, Arabidopsis thaliana (P42745)
-
brenda
Wang, J.; Taherbhoy, A.M.; Hunt, H.W.; Seyedin, S.N.; Miller, D.W., Miller, D.J.; Huang, D.T.; Schulman, B.A.
Crystal structure of UBA2ufd-Ubc9: Insights into E1-E2 interactions in Sumo pathways
PLoS ONE
1
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Saccharomyces cerevisiae (P50623), Saccharomyces cerevisiae
brenda
Chung, E.; Cho, C.W.; So, H.A.; Kang, J.S.; Chung, Y.S.; Lee, J.H.
Overexpression of VrUBC1, a mung bean E2 Ubiquitin-conjugating enzyme, enhances osmotic stress tolerance in Arabidopsis
PLoS One
8
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2013
Vigna radiata (D2D3G0)
brenda
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
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Homo sapiens (P63279)
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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
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53
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Homo sapiens (Q969T4)
brenda
Horikoshi, Y.; Habu, T.; Matsumoto, T.
An E2 enzyme Ubc11 is required for ubiquitination of Slp1/Cdc20 and spindle checkpoint silencing in fission yeast
Cell Cycle
12
961-971
2013
Schizosaccharomyces pombe (O00103), Schizosaccharomyces pombe, Schizosaccharomyces pombe 972 (O00103)
brenda
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HECT-E3 ligase ETC-1 regulates securin and cyclin B1 cytoplasmic abundance to promote timely anaphase during meiosis in C. elegans
Development
140
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Caenorhabditis elegans (Q21633), Caenorhabditis elegans
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Homo sapiens
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282
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Homo sapiens
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The HECT domain of TRIP12 ubiquitinates substrates of the ubiquitin fusion degradation pathway
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Homo sapiens (P51668)
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Koenig, P.A.; Nicholls, P.K.; Schmidt, F.I.; Hagiwara, M.; Maruyama, T.; Frydman, G.H.; Watson, N.; Page, D.C.; Ploegh, H.L.
The E2 ubiquitin-conjugating enzyme UBE2J1 is required for spermiogenesis in mice
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289
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Mus musculus (Q9JJZ4)
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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
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290
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Homo sapiens (P62253)
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A specific subset of E2 ubiquitin-conjugating enzymes regulate Parkin activation and mitophagy differently
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Homo sapiens
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Wen, R.; Wang, S.; Xiang, D.; Venglat, P.; Shi, X.; Zang, Y.; Datla, R.; Xiao, W.; Wang, H.
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80
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Arabidopsis thaliana (Q94A97)
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Cohen, I.; Wiener, R.; Reiss, Y.; Ravid, T.
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Saccharomyces cerevisiae (Q02159), Saccharomyces cerevisiae
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A disulphide bond in the E2 enzyme Pex4p modulates ubiquitin-conjugating activity
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3
2212
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Saccharomyces cerevisiae (P29340), Saccharomyces cerevisiae
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Antonie van Leeuwenhoek
104
509-520
2013
Gemmata obscuriglobus, Pirellula staleyi, Pirellula staleyi DSM 6068
brenda
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54
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Homo sapiens
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Homo sapiens
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6
1019
2015
Solanum peruvianum
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A newly discovered ubiquitin-conjugating enzyme E2 correlated with the cryogenic autolysis of Volvariella volvacea
Gene
583
58-63
2016
Volvariella volvacea, Volvariella volvacea V23
brenda
Qi, C.; Li, D.F.; Feng, L.; Hou, Y.; Sun, H.; Wang, D.C.; Liu, W.
Biochemical and structural characterization of a novel ubiquitin-conjugating enzyme E2 from Agrocybe aegeria reveals Ube2w family-specific properties
Sci. Rep.
5
16056
2015
Cyclocybe aegerita
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Imura, Y.; Molho, M.; Chuang, C.; Nagy, P.D.
Cellular Ubc2/Rad6 E2 ubiquitin-conjugating enzyme facilitates tombusvirus replication in yeast and plants
Virology
484
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Arabidopsis thaliana, Saccharomyces cerevisiae, Saccharomyces cerevisiae BY4741
brenda
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)
brenda
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.
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55
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Homo sapiens (P63279)
brenda
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
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2019
Homo sapiens (P60604), Homo sapiens (Q8N2K1), Homo sapiens (Q9Y385), Homo sapiens
brenda
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)
brenda
Alpi, A.F.; Chaugule, V.; Walden, H.
Mechanism and disease association of E2-conjugating enzymes lessons from UBE2T and UBE2L3
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473
3401-3419
2016
Homo sapiens (P68036), Homo sapiens (Q9NPD8)
brenda
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
brenda
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)
brenda
Mizushima, N.
The ubiquitin E2 enzyme UBE2QL1 mediates lysophagy
EMBO Rep.
20
e49104
2019
Homo sapiens (A1L167)
brenda
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)
brenda
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)
brenda
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
brenda
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)
brenda
Hagiwara, M.; Ling, J.; Koenig, P.A.; Ploegh, H.L.
Posttranscriptional regulation of glycoprotein quality control in the endoplasmic reticulum is controlled by the E2 Ub-conjugating enzyme UBC6e
Mol. Cell
63
753-767
2016
Mus musculus (Q9JJZ4)
brenda
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)
brenda
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
Homo sapiens (P49427), Saccharomyces cerevisiae (P14682), Saccharomyces cerevisiae ATCC 204508 (P14682)
brenda
Gao, Y.; Wang, Y.; Xin, H.; Li, S.; Liang, Z.
Involvement of ubiquitin-conjugating enzyme (E2 gene family) in ripening process and response to cold and heat stress of Vitis vinifera
Sci. Rep.
7
13290
2017
Vitis vinifera
brenda
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)
brenda
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)
brenda
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