2.3.2.23: E2 ubiquitin-conjugating enzyme
This is an abbreviated version!
For detailed information about E2 ubiquitin-conjugating enzyme, go to the full flat file.
Word Map on EC 2.3.2.23
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2.3.2.23
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proteasome
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ligases
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polyubiquitination
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sumoylation
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ubiquitin-like
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finger
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ubiquitin-proteasome
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ubiquitylation
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monoubiquitination
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ubiquitin-protein
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ubiquitin-activating
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k63-linked
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ubiquitin-dependent
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cullins
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parkin
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ubiquitin-mediated
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ubiquitin-related
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fanconi
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anaphase-promoting
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deubiquitinating
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cullin-ring
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isopeptide
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error-free
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isg15
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lys63-linked
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neddylation
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cdc20
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sumo1
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autoubiquitination
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traf6
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er-associated
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ring-h2
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ranbp2
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tak1
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thiolester
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ring-finger
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sic1
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e3-ligase
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multiubiquitination
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tpx2
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rbx1
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translesion
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fancd2
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aurka
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postreplication
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conjugase
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ubiquitin-binding
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ubiquitin-ligase
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ring-type
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medicine
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nonerythroid
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diagnostics
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drug development
- 2.3.2.23
- proteasome
- ligases
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polyubiquitination
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sumoylation
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ubiquitin-like
- finger
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ubiquitin-proteasome
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ubiquitylation
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monoubiquitination
- ubiquitin-protein
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ubiquitin-activating
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k63-linked
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ubiquitin-dependent
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cullins
- parkin
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ubiquitin-mediated
-
ubiquitin-related
-
fanconi
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anaphase-promoting
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deubiquitinating
-
cullin-ring
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isopeptide
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error-free
- isg15
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lys63-linked
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neddylation
- cdc20
- sumo1
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autoubiquitination
- traf6
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er-associated
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ring-h2
- ranbp2
- tak1
- thiolester
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ring-finger
- sic1
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e3-ligase
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multiubiquitination
- tpx2
- rbx1
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translesion
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fancd2
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aurka
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postreplication
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conjugase
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ubiquitin-binding
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ubiquitin-ligase
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ring-type
- medicine
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nonerythroid
- diagnostics
- drug development
Reaction
Synonyms
alpha spectrin, ARIH1, At1g78870, At2g02760, CDC34, Cdc34B, Ci0100152677, E2 enzyme, E2 Ub-conjugating enzyme, E2 ubiquitin conjugating enzyme, E2 ubiquitin-conjugating enzyme, E2-20K, E2-25K, E2-conjugating enzyme, E2-ubiquitin conjugating enzyme, FANCT, HOYS7, Mms2, NCUBE1, NEDD8-activating enzyme E1 catalytic subunit, Pex4, Rad6a, RAD6B, Rad6p, SCEI, SUMO E2 conjugating enzyme, SUMO E2 enzyme, SUMO-1-conjugating enzyme Ubc9, SUMO-conjugating enzyme UBC9, UBA2, Uba3, UBA6-specific E2 enzyme 1, UBC E2, Ubc-18, Ubc1, Ubc11, Ubc13, Ubc2, Ubc35, Ubc3B, Ubc4, Ubc4/5, Ubc5a, Ubc6, UBC6e, UBC7, Ubc8, Ubc9, UbcA1, UBCE4, UbcH10, UBCH2, UbcH3, UbcH5A, UbcH5B, UbcH5C, UbcH5D, UbcH6, UbcH7, UbcH8, UbcH9, UbcM2, UbcM4, Ube2, UBE2A, UBE2B, UBE2C, UBE2D, UBE2D1, ube2d1b, UBE2D2, UBE2D3, UBE2D4, UBE2E1, UBE2E2, UBE2E3, Ube2G, UBE2G1, UBE2G2, UBE2H, Ube2I, Ube2J1, UBE2J2, UBE2K, UBE2L3, UBE2L6, UBE2N, Ube2NL, UBE2Q1, UBE2Q2, UBE2QL, UBE2QL1, Ube2r, UBE2R1, UBE2R2, UBE2S, UBE2T, UBE2U, Ube2V, UBE2V1, UBE2V2, UBE2W, UBE2Z, ubiquitin-conjugating enzyme, ubiquitin-conjugating enzyme (E2), ubiquitin-conjugating enzyme E2, ubiquitin-conjugating enzyme E2 B, ubiquitin-conjugating enzyme E2 D1, ubiquitin-conjugating enzyme E2 G1, ubiquitin-conjugating enzyme E2 Z, ubiquitin-conjugating enzyme E2-20 kDa, ubiquitin-conjugating enzyme E2T, ubiquitination enzyme, Uev1, Uev1A, Uev2, USE1, VvUBC
ECTree
2.3.2.23 E2 ubiquitin-conjugating enzymeAdvanced search results
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results (Substrates Products
Substrates Products on EC 2.3.2.23 - E2 ubiquitin-conjugating enzyme
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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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-
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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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-
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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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-
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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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-
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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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-
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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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-
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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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-
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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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-
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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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-
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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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-
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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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-
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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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-
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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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-
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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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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
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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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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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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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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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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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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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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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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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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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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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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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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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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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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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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
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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
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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
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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
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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
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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
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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
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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
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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
?
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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
?
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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
?
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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
?
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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
?
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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
?
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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
?
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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
?
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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
?
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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
?
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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 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
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additional information
?
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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
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additional information
?
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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
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additional information
?
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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
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-
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additional information
?
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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
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-
-
additional information
?
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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
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-
-
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
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-
-
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
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-
-
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
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additional information
?
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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)
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-
-
additional information
?
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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)
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-
-
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)
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-
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additional information
?
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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)
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-
-
additional information
?
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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)
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-
-
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)
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-
-
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)
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-
-
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)
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-
-
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)
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-
-
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)
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-
-
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)
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-
-
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)
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-
-
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)
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-
-
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)
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-
-
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)
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-
-
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)
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-
-
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)
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-
-
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)
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-
-
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)
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-
-
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)
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-
-
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)
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-
-
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)
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-
-
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)
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-
-
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)
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-
-
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)
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-
-
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)
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-
-
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)
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-
-
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)
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-
-
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)
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-
-
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)
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additional information
?
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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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the Ube2R1/2 acidic loop participates in Lys48-specific polyubiquitin chain formation by binding to Skp1-cullin-Fbox (SCF), kinetics
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