2.3.2.24: (E3-independent) E2 ubiquitin-conjugating enzyme
This is an abbreviated version!
For detailed information about (E3-independent) E2 ubiquitin-conjugating enzyme, go to the full flat file.
Word Map on EC 2.3.2.24
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2.3.2.24
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proteasome
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cyclins
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ligases
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polyubiquitination
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mitotic
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ubiquitin-proteasome
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anaphase-promoting
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spindle
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omnibus
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cdc20
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ubiquitin-dependent
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ubiquitin-mediated
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cullin
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sic1
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scfcdc4
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autoubiquitination
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anaphase
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aurka
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cullin-ring
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rad6
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e2-conjugating
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tpx2
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rbx1
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ubch6
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scf-mediated
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multiubiquitination
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nusap1
- 2.3.2.24
- proteasome
- cyclins
- ligases
-
polyubiquitination
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mitotic
-
ubiquitin-proteasome
-
anaphase-promoting
- spindle
-
omnibus
- cdc20
-
ubiquitin-dependent
-
ubiquitin-mediated
-
cullin
- sic1
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scfcdc4
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autoubiquitination
-
anaphase
-
aurka
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cullin-ring
- rad6
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e2-conjugating
- tpx2
- rbx1
- ubch6
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scf-mediated
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multiubiquitination
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nusap1
Reaction
Synonyms
arsenite-sensitive E2, biquitin carrier protein D4, biquitin-conjugating enzyme E2 T, CDC34, CLF_100482, E2 ubiquitin-conjugating enzyme, E2-230K, E2-EPF ubiquitin carrier protein, E2-EPF UCP, E2/E3 hybrid enzyme, E2230K, HIP2, N-terminus-conjugating E2, UB carrier protein (E2), Ubc1, Ubc3, UbcH10, UBE2A, UBE2B, UBE2C, UBE2D1, UBE2D2, UBE2D3, UBE2D4, UBE2E1, UBE2E2, UBE2E3, UBE2G1, UBE2G2, UBE2H, UBE2K, UBE2L3, UBE2N, UBE2O, UBE2Q2, UBE2R1, UBE2R2, UBE2S, UBE2T, UBE2V1, UBE2V2, UBE2W, ubiquitin carrier protein A, ubiquitin carrier protein B, ubiquitin carrier protein C, ubiquitin carrier protein D1, ubiquitin carrier protein D2, ubiquitin carrier protein D3, Ubiquitin carrier protein E1, ubiquitin carrier protein E2, ubiquitin carrier protein E3, Ubiquitin carrier protein G1, Ubiquitin carrier protein G2, ubiquitin carrier protein H, Ubiquitin carrier protein L3, ubiquitin carrier protein N, Ubiquitin carrier protein Q2, ubiquitin carrier protein R2, ubiquitin carrier protein S, ubiquitin carrier protein T, ubiquitin carrier protein W, ubiquitin-conjugating enzyme E2, ubiquitin-conjugating enzyme E2 A, ubiquitin-conjugating enzyme E2 B, ubiquitin-conjugating enzyme E2 C, ubiquitin-conjugating enzyme E2 D1, ubiquitin-conjugating enzyme E2 D2, ubiquitin-conjugating enzyme E2 D3, ubiquitin-conjugating enzyme E2 D4, ubiquitin-conjugating enzyme E2 E1, ubiquitin-conjugating enzyme E2 E2, ubiquitin-conjugating enzyme E2 E3, ubiquitin-conjugating enzyme E2 G1, ubiquitin-conjugating enzyme E2 G2, ubiquitin-conjugating enzyme E2 H, ubiquitin-conjugating enzyme E2 K, ubiquitin-conjugating enzyme E2 L3, ubiquitin-conjugating enzyme E2 N, ubiquitin-conjugating enzyme E2 O, Ubiquitin-conjugating enzyme E2 Q2, ubiquitin-conjugating enzyme E2 R1, ubiquitin-conjugating enzyme E2 R2, ubiquitin-conjugating enzyme E2 S, ubiquitin-conjugating enzyme E2 variant 1, ubiquitin-conjugating enzyme E2 variant 2, ubiquitin-conjugating enzyme E2 W, ubiquitin-conjugating enzyme E2-25 kDa, ubiquitin-conjugating enzyme E2-CDC34
ECTree
2.3.2.24 (E3-independent) E2 ubiquitin-conjugating enzymeAdvanced search results
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results (Substrates Products
Substrates Products on EC 2.3.2.24 - (E3-independent) 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
2 N6-monoubiquitinyl-[Ubc1]-L-lysine
N6-diubiquitinyl-[Ubc1]-L-lysine + [Ube2K]-L-lysine
-
-
-
?
2 N6-monoubiquitinyl-[Ube2K]-L-lysine
N6-diubiquitinyl-[Ube2K]-L-lysine + [Ube2K]-L-lysine
-
-
-
?
S-ubiquitinyl-[E1 ubiquitin-activating enzyme]-L-cysteine + L-lysine
[E1 ubiquitin-activating enzyme]-L-cysteine + N6-monoubiquitinyl-L-lysine
-
-
-
-
?
S-ubiquitinyl-[E1 ubiquitin-activating enzyme]-L-cysteine + N6-(ubiquitin)n-[E2 enzyme CDC34]-L-lysine
[E1 ubiquitin-activating enzyme]-L-cysteine + N6-(ubiquitin)(n+1)-[E2 enzyme CDC34]-L-lysine
-
-
CDC34 mutants differ in the extent of multiubiquitination they catalyze during an autoubiquitination reaction
-
?
S-ubiquitinyl-[E1 ubiquitin-activating enzyme]-L-cysteine + N6-(ubiquitin)n-[histone H2A]-L-lysine
[E1 ubiquitin-activating enzyme]-L-cysteine + N6-(ubiquitin)(n+1)-[histone H2A]-L-lysine
-
reaction does not require additional factors such as E3 enzyme but depends on the E1 and ATP
-
?
S-ubiquitinyl-[E1 ubiquitin-activating enzyme]-L-cysteine + S-(ubiquitin)n-Ube2g2-L-cysteine
[E1 ubiquitin-activating enzyme]-L-cysteine + S-(ubiquitin)(n+1)-Ube2g2-L-cysteine
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short chains of polyubiquitins can be linked bonds to E2 enzyme Ube2g2
-
?
S-ubiquitinyl-[E1 ubiquitin-activating enzyme]-L-cysteine + S-(ubiquitin)n-Ube2K-L-cysteine
[E1 ubiquitin-activating enzyme]-L-cysteine + S-(ubiquitin)(n+1)-Ube2K-L-cysteine
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longer chains of polyubiquitins can be linked bonds to E2 enzyme Ube2K. Ubiquitin chains are assembled on the active site cysteine of Ube2K through thioester bond
-
?
S-ubiquitinyl-[E1 ubiquitin-activating enzyme]-L-cysteine + UbcH10-L-cysteine
[E1 ubiquitin-activating enzyme]-L-cysteine + S-monoubiquitinyl-UbcH10-L-cysteine
-
-
-
?
S-ubiquitinyl-[E1 ubiquitin-activating enzyme]-L-cysteine + Ube2g2-L-cysteine
[E1 ubiquitin-activating enzyme]-L-cysteine + S-monoubiquitinyl-Ube2g2-L-cysteine
-
-
-
?
S-ubiquitinyl-[E1 ubiquitin-activating enzyme]-L-cysteine + Ube2K-L-cysteine
[E1 ubiquitin-activating enzyme]-L-cysteine + S-monoubiquitinyl-Ube2K-L-cysteine
-
-
-
?
S-ubiquitinyl-[E1 ubiquitin-activating enzyme]-L-cysteine + [cytochrome c]-L-lysine
[E1 ubiquitin-activating enzyme]-L-cysteine + N6-monoubiquitinyl-[cytochrome c]-L-lysine lysine
-
-
approximate relative activities as ubiquitin acceptors are: histones H2A:H2B:cytochrome c 1:0.5:0.2
-
?
S-ubiquitinyl-[E1 ubiquitin-activating enzyme]-L-cysteine + [E2 enzyme CDC34]-L-lysine
[E1 ubiquitin-activating enzyme]-L-cysteine + N6-monoubiquitinyl-[E2 enzyme CDC34]-L-lysine
-
-
CDC34 mutants differ in the extent of multiubiquitination they catalyze during an autoubiquitination reaction
-
?
S-ubiquitinyl-[E1 ubiquitin-activating enzyme]-L-cysteine + [histone H1]-L-lysine
[E1 ubiquitin-activating enzyme]-L-cysteine + N6-monoubiquitinyl-[histone H1]-L-lysine
-
-
significant rates of processive multiple ubiquitination of calf thymus H1 are catalyzed by E2 enzymes of 14 kDa, 20 kDa, and 32 kDa
-
?
S-ubiquitinyl-[E1 ubiquitin-activating enzyme]-L-cysteine + [histone H2A]-L-lysine
[E1 ubiquitin-activating enzyme]-L-cysteine + N6-monoubiquitinyl-[histone H2A]-L-lysine
S-ubiquitinyl-[E1 ubiquitin-activating enzyme]-L-cysteine + [histone H2B]-L-lysine
[E1 ubiquitin-activating enzyme]-L-cysteine + N6-monoubiquitinyl-[histone H2B]-L-lysine
S-ubiquitinyl-[E1 ubiquitin-activating enzyme]-L-cysteine + [histone H2B]-L-lysine
[E1 ubiquitin-activating enzyme]-L-cysteine + N6-monoubiquitinyl-[histone H2B]-L-lysine lysine
-
-
approximate relative activities as ubiquitin acceptors are: histones H2A:H2B:cytochrome c 1:0.5:0.2
-
?
S-ubiquitinyl-[E1 ubiquitin-activating enzyme]-L-cysteine + [histone H3]-L-lysine
[E1 ubiquitin-activating enzyme]-L-cysteine + N6-monoubiquitinyl-[histone H3]-L-lysine
-
-
significant rates of nonprocessive core histone monoubiquitination are catalyzed by E2 enzymes of 14 kDa, 20 kDa, and 32 kDa
-
?
S-ubiquitinyl-[E1 ubiquitin-activating enzyme]-L-cysteine + [histone H4]-L-lysine
[E1 ubiquitin-activating enzyme]-L-cysteine + N6-monoubiquitinyl-[histone H4]-L-lysine
-
-
significant rates of nonprocessive core histone monoubiquitination are catalyzed by E2 enzymes of 14 kDa, 20 kDa, and 32 kDa
-
?
[E1 ubiquitin-activating enzyme]-S-ubiquitinyl-L-cysteine + [acceptor protein]-L-lysine
[E1 ubiquitin-activating enzyme]-L-cysteine + [acceptor protein]-N6-monoubiquitinyl-L-lysine
[E1 ubiquitin-activating enzyme]-S-ubiquitinyl-L-cysteine + [AMPKalpha2]-L-lysine48
[E1 ubiquitin-activating enzyme]-L-cysteine + [AMPKalpha2 ]-N6-monoubiquitinyl-L-lysine48
polyubiquitination of AMPKalpha2
-
-
?
[E1 ubiquitin-activating enzyme]-S-ubiquitinyl-L-cysteine + [AMPKalpha2]-L-lysine48
[E1 ubiquitin-activating enzyme]-L-cysteine + [AMPKalpha2]-N6-monoubiquitinyl-L-lysine48
-
-
-
?
[E1 ubiquitin-activating enzyme]-S-ubiquitinyl-L-cysteine + [BAP1]-L-lysine
[E1 ubiquitin-activating enzyme]-L-cysteine + [BAP1]-N6-monoubiquitinyl-L-lysine
UBE2O promotes multi-monoubiquitination on BAP1. The ubiquitination of BAP1 requires both the N-terminal CR1-CR2 domain and the C-terminal UBC domain of UBE2O. The absence of either domain completely abolishes BAP1 ubiquitination
-
-
?
[E1 ubiquitin-activating enzyme]-S-ubiquitinyl-L-cysteine + [BMAL1]-L-lysine
[E1 ubiquitin-activating enzyme]-L-cysteine + [BMAL1]-N6-monoubiquitinyl-L-lysine
[E1 ubiquitin-activating enzyme]-S-ubiquitinyl-L-cysteine + [c-Maf]-L-lysine
[E1 ubiquitin-activating enzyme]-L-cysteine + [acceptor c-Maf]-N6-monoubiquitinyl-L-lysine
polyubiquitination of o-Maf
-
-
?
[E1 ubiquitin-activating enzyme]-S-ubiquitinyl-L-cysteine + [Hippel-Lindau protein]-L-lysine
[E1 ubiquitin-activating enzyme]-L-cysteine + [Hippel-Lindau protein]-N6-monoubiquitinyl-L-lysine
[E1 ubiquitin-activating enzyme]-S-ubiquitinyl-L-cysteine + [MLL protein]-L-lysine
[E1 ubiquitin-activating enzyme]-L-cysteine + [MLL protein]-N6-monoubiquitinyl-L-lysine
polyubiquitination of protein MLL
-
-
?
[E1 ubiquitin-activating enzyme]-S-ubiquitinyl-L-cysteine + [SMAD6]-L-lysine
[E1 ubiquitin-activating enzyme]-L-cysteine + [SMAD6]-N6-monoubiquitinyl-L-lysine
monoubiquitination of SMAD6
-
-
?
[E1 ubiquitin-activating enzyme]-S-ubiquitinyl-L-cysteine + [TRAF6]-L-lysine63
[E1 ubiquitin-activating enzyme]-L-cysteine + [TRAF6]-N6-monoubiquitinyl-L-lysine63
polyubiquitination of TRAF6 K63
-
-
?
[ubiquitin-carrier protein E2]-S-ubiquitinyl-L-cysteine + [alpha-casein]-L-lysine
[ubiquitin-carrier protein E2]-L-cysteine + [alpha-casein]-N6-ubiquitinyl-L-lysine
-
42% relative activity compared to cytochrome c as substrate
-
-
?
[ubiquitin-carrier protein E2]-S-ubiquitinyl-L-cysteine + [alpha-lactalbumin]-L-lysine
[ubiquitin-carrier protein E2]-L-cysteine + [alpha-lactalbumin]-N6-ubiquitinyl-L-lysine
-
12% with human and 15% with bovine alpha-lactalbumin, relative activity compared to cytochrome c as substrate
-
-
?
[ubiquitin-carrier protein E2]-S-ubiquitinyl-L-cysteine + [cytochrome c]-L-lysine
[ubiquitin-carrier protein E2]-L-cysteine + [cytochrome c]-N6-ubiquitinyl-L-lysine
-
yeast cytochrome c, ubiquitin from human blood
-
-
?
[ubiquitin-carrier protein E2]-S-ubiquitinyl-L-cysteine + [histone H3]-L-lysine
[ubiquitin-carrier protein E2]-L-cysteine + [histone H3]-N6-ubiquitinyl-L-lysine
-
-
-
-
?
[ubiquitin-carrier protein E2]-S-ubiquitinyl-L-cysteine + [lysozyme]-L-lysine
[ubiquitin-carrier protein E2]-L-cysteine + [lysozyme]-N6-ubiquitinyl-L-lysine
-
5% relative activity compared to cytochrome c as substrate
-
-
?
[ubiquitin-carrier protein UbcH2]-S-ubiquitinyl-L-cysteine + [Eps15]-L-lysine
[ubiquitin-carrier protein UbcH2]-L-cysteine + [Eps15]-N6-ubiquitinyl-L-lysine
-
substrate protein Eps15 contains two C-terminal ubiquitin-interacting motifs. It is potently ubiquitinated by UbcH5 isoforms and less well by UbcH2 and UbcH6
-
-
?
[ubiquitin-carrier protein UbcH2]-S-ubiquitinyl-L-cysteine + [Pol k]-L-lysine
[ubiquitin-carrier protein UbcH2]-L-cysteine + [Pol k]-N6-ubiquitinyl-L-lysine
-
substrate protein Pol k contains two C-terminal ubiquitin-binding zinc finger domains. It is ubiquitinated by UbcH2, UbcH5 isoforms and UbcH6
-
-
?
[ubiquitin-carrier protein UbcH5A]-S-ubiquitinyl-L-cysteine + [Stam2]-L-lysine
[ubiquitin-carrier protein UbcH5A]-L-cysteine + [Stam6]-N6-ubiquitinyl-L-lysine
-
substrate protein Stam2 contains a N-terminal ubiquitin-interacting motif and VHS domain, it is most strongly ubiquitinated by E2 isoform UbcH5A
-
-
?
[ubiquitin-carrier protein UbcH5]-S-ubiquitinyl-L-cysteine + [Eps15]-L-lysine
[ubiquitin-carrier protein UbcH5]-L-cysteine + [Eps15]-N6-ubiquitinyl-L-lysine
-
substrate protein Eps15 contains two C-terminal ubiquitin-interacting motifs. It is potently ubiquitinated by UbcH5 isoforms and less well by UbcH2 and UbcH6
-
-
?
[ubiquitin-carrier protein UbcH5]-S-ubiquitinyl-L-cysteine + [Pol k]-L-lysine
[ubiquitin-carrier protein UbcH5]-L-cysteine + [Pol k]-N6-ubiquitinyl-L-lysine
-
substrate protein Pol k contains two C-terminal ubiquitin-binding zinc finger domains. It is ubiquitinated by UbcH2, UbcH5 isoforms and UbcH6
-
-
?
[ubiquitin-carrier protein UbcH5]-S-ubiquitinyl-L-cysteine + [Pol tau]-L-lysine
[ubiquitin-carrier protein UbcH5]-L-cysteine + [Pol tau]-N6-ubiquitinyl-L-lysine
-
substrate protein Pol tau contains two C-terminal ubiquitin-associated domains. It is ubiquitinated by all E2 isoforms tested
-
-
?
[ubiquitin-carrier protein UbcH6]-S-ubiquitinyl-L-cysteine + [Eps15]-L-lysine
[ubiquitin-carrier protein UbcH6]-L-cysteine + [Eps15]-N6-ubiquitinyl-L-lysine
-
substrate protein Eps15 contains two C-terminal ubiquitin-interacting motifs. It is potently ubiquitinated by UbcH5 isoforms and less well by UbcH2 and UbcH6
-
-
?
[ubiquitin-carrier protein UbcH6]-S-ubiquitinyl-L-cysteine + [Pol k]-L-lysine
[ubiquitin-carrier protein UbcH6]-L-cysteine + [Pol k]-N6-ubiquitinyl-L-lysine
-
substrate protein Pol k contains two C-terminal ubiquitin-binding zinc finger domains. It is ubiquitinated by UbcH2, UbcH5 isoforms and UbcH6
-
-
?
S-ubiquitinyl-[E1 ubiquitin-activating enzyme]-L-cysteine + [histone H2A]-L-lysine
[E1 ubiquitin-activating enzyme]-L-cysteine + N6-monoubiquitinyl-[histone H2A]-L-lysine
-
reaction does not require additional factors such as E3 enzyme but depends on the E1 and ATP
-
?
S-ubiquitinyl-[E1 ubiquitin-activating enzyme]-L-cysteine + [histone H2A]-L-lysine
[E1 ubiquitin-activating enzyme]-L-cysteine + N6-monoubiquitinyl-[histone H2A]-L-lysine
-
-
approximate relative activities as ubiquitin acceptors are: histones H2A:H2B:cytochrome c 1:0.5:0.2
-
?
S-ubiquitinyl-[E1 ubiquitin-activating enzyme]-L-cysteine + [histone H2A]-L-lysine
[E1 ubiquitin-activating enzyme]-L-cysteine + N6-monoubiquitinyl-[histone H2A]-L-lysine
-
-
significant rates of nonprocessive core histone monoubiquitination are catalyzed by E2 enzymes of 14 kDa, 20 kDa, and 32 kDa
-
?
S-ubiquitinyl-[E1 ubiquitin-activating enzyme]-L-cysteine + [histone H2B]-L-lysine
[E1 ubiquitin-activating enzyme]-L-cysteine + N6-monoubiquitinyl-[histone H2B]-L-lysine
-
-
significant rates of nonprocessive core histone monoubiquitination are catalyzed by E2 enzymes of 14 kDa, 20 kDa, and 32 kDa
-
?
S-ubiquitinyl-[E1 ubiquitin-activating enzyme]-L-cysteine + [histone H2B]-L-lysine
[E1 ubiquitin-activating enzyme]-L-cysteine + N6-monoubiquitinyl-[histone H2B]-L-lysine
-
-
isoform CDC34 mutant proteins expressed in Escherichia coli display E3-independent ubiquitin-conjugating activity
-
?
[E1 ubiquitin-activating enzyme]-S-ubiquitinyl-L-cysteine + [acceptor protein]-L-lysine
[E1 ubiquitin-activating enzyme]-L-cysteine + [acceptor protein]-N6-monoubiquitinyl-L-lysine
-
-
-
?
[E1 ubiquitin-activating enzyme]-S-ubiquitinyl-L-cysteine + [acceptor protein]-L-lysine
[E1 ubiquitin-activating enzyme]-L-cysteine + [acceptor protein]-N6-monoubiquitinyl-L-lysine
-
-
-
-
?
[E1 ubiquitin-activating enzyme]-S-ubiquitinyl-L-cysteine + [acceptor protein]-L-lysine
[E1 ubiquitin-activating enzyme]-L-cysteine + [acceptor protein]-N6-monoubiquitinyl-L-lysine
-
-
-
?
[E1 ubiquitin-activating enzyme]-S-ubiquitinyl-L-cysteine + [BMAL1]-L-lysine
[E1 ubiquitin-activating enzyme]-L-cysteine + [BMAL1]-N6-monoubiquitinyl-L-lysine
mapping of the BMAL1-interacting domain in UBE2O
-
-
?
[E1 ubiquitin-activating enzyme]-S-ubiquitinyl-L-cysteine + [BMAL1]-L-lysine
[E1 ubiquitin-activating enzyme]-L-cysteine + [BMAL1]-N6-monoubiquitinyl-L-lysine
polyubiquitination of BMAL1
-
-
?
[E1 ubiquitin-activating enzyme]-S-ubiquitinyl-L-cysteine + [BMAL1]-L-lysine
[E1 ubiquitin-activating enzyme]-L-cysteine + [BMAL1]-N6-monoubiquitinyl-L-lysine
polyubiquitination of hydrocarbon receptor nuclear translocator-like protein 1 (Arntl or Bmal1). The critical Cys residue in the CR2 domain of UBE2O is responsible for BMAL1 ubiquitination
-
-
?
[E1 ubiquitin-activating enzyme]-S-ubiquitinyl-L-cysteine + [Hippel-Lindau protein]-L-lysine
[E1 ubiquitin-activating enzyme]-L-cysteine + [Hippel-Lindau protein]-N6-monoubiquitinyl-L-lysine
-
-
-
?
[E1 ubiquitin-activating enzyme]-S-ubiquitinyl-L-cysteine + [Hippel-Lindau protein]-L-lysine
[E1 ubiquitin-activating enzyme]-L-cysteine + [Hippel-Lindau protein]-N6-monoubiquitinyl-L-lysine
the polyubiquitin chain formation on Hippel-Lindau protein (pVHL) occurrs on all three of its lysines (Lys159, Lys171 and Lys196)
-
-
?
additional information
?
-
-
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
-
?
additional information
?
-
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
-
?
additional information
?
-
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
-
?
additional information
?
-
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
-
?
additional information
?
-
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
-
?
additional information
?
-
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
-
?
additional information
?
-
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
-
?
additional information
?
-
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
-
?
additional information
?
-
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
-
?
additional information
?
-
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
-
?
additional information
?
-
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
-
?
additional information
?
-
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
-
?
additional information
?
-
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
-
?
additional information
?
-
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
-
?
additional information
?
-
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
-
?
additional information
?
-
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
-
?
additional information
?
-
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
-
?
additional information
?
-
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
-
?
additional information
?
-
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
-
?
additional information
?
-
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
-
?
additional information
?
-
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
-
?
additional information
?
-
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
-
?
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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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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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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the presence of ubiquitin-binding domains (UBDs) allows the ubiquitination of host proteins independently of E3 ligases. UBDs of different types, including ubiquitin-interacting motif UIM, ubiquitin-associated domain UBM, and ubiquitin-binding zinc finger domain UBZ, can directly cooperate with ubiquitin-charged E2 enzymes to promote monoubiquitination. Ubiquitin-loaded E2 and substrates interact in cells and E2 enzymes are essential for their monoubiquitination in vivo. This modification is mechanistically and functionally distinct from E3-mediated and growth factor-dependent monoubiquitination. The ability to transfer ubiquitin to a substrate is a common feature of all tested E2 enzymes. However, E2 enzymes show substrate specificity
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E3-independent ubiquitination by Ube2K produces unanchored but also Ube2K-linked polyubiquitins through thioester and isopeptide bonds. E3-independent assembly of polyubiquitins on the catalytic cysteine of Ube2K strongly supports the possibility of en bloc transfer for polyubiquitination. Different lengths of polyubiquitins are linked to different E2s through thioester bond. In vitro E3-independent ubiquitination by Ube2K simultaneously produces unanchored, isopeptde-linked, and thioester-linked polyubiquitin chains
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E3-independent ubiquitination by Ube2K produces unanchored but also Ube2K-linked polyubiquitins through thioester and isopeptide bonds. E3-independent assembly of polyubiquitins on the catalytic cysteine of Ube2K strongly supports the possibility of en bloc transfer for polyubiquitination. Different lengths of polyubiquitins are linked to different E2s through thioester bond. In vitro E3-independent ubiquitination by Ube2K simultaneously produces unanchored, isopeptde-linked, and thioester-linked polyubiquitin chains
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additional information
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E3-independent ubiquitination by Ube2K produces unanchored but also Ube2K-linked polyubiquitins through thioester and isopeptide bonds. E3-independent assembly of polyubiquitins on the catalytic cysteine of Ube2K strongly supports the possibility of en bloc transfer for polyubiquitination. Different lengths of polyubiquitins are linked to different E2s through thioester bond. In vitro E3-independent ubiquitination by Ube2K simultaneously produces unanchored, isopeptde-linked, and thioester-linked polyubiquitin chains
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isoform UbcH10 does not preassemble polyubiquitin chains on its acitve site cysteine
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isoform UbcH10 does not preassemble polyubiquitin chains on its acitve site cysteine
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isoform UbcH10 does not preassemble polyubiquitin chains on its acitve site cysteine
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ubiquitin thiol ester forms of at least four of five E2s tested catalyze ubiquitin transfer to a number of small amines, in a reaction that does not require E3 enzyme, and only primary amines on primary carbons can serve as ubiquitin acceptors. E3-independent ubiquitin transfer to the small, basic proteins histones H2A and H2B, and cytochrome c, is also observed
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E2-EPF ubiquitin carrier protein (UCP) possesses E3 ubiquitin ligase activity via its cysteine 118 residue. E2-EPF UCP elongates E3-independent polyubiquitin chains on the lysine residues of von Hippel-Lindau protein (pVHL) and its own lysine residues both in vitro and in vivo. The initiation of the ubiquitin reaction depends on not only Lys11 linkage but also the Lys6, Lys48 and Lys63 residues of ubiquitin, which are involved in polyubiquitin chain formation on UCP itself. UCP self-association occurred through the UBC domain, which also contributes to the interaction with pVHL. The polyubiquitin chains appears on the N-terminus of UCP in vivo, which indicates that the N-terminus of UCP contains target lysines for polyubiquitination. The Lys76 residue of UCP is the most critical site for auto-ubiquitination, whereas the polyubiquitin chain formation on pVHL occurrs on all three of its lysines (Lys159, Lys171 and Lys196). Polyubiquitin chain formation requires the coordination of Cys95 and Cys118 between two interacting molecules. The mechanism of the polyubiquitin chain reaction of UCP may involve the transfer of ubiquitin from Cys95 to Cys118 by trans-thiolation, with polyubiquitin chains forming at Cys118 by reversible thioester bonding. The polyubiquitin chains are then moved to the lysine residues of the substrate by irreversible isopeptide bonding. During the elongation of the ubiquitin chain, an active Cys118 residue is required in both parts of UCP, namely, the catalytic enzyme and the substrate
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the enzyme interacts with E3 ligases of types RING and RBR, and with its own N-terminus
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UBE2O is an E2/E3 hybrid enzyme and exhibits both the E2 and E3 activities. UBE2O performs monoubiquitination, multi-monoubiquitination, and polyubiquitination of different substrates, mechanisms, overview. A consensus sequence analysis of the UBE2O-mediated ubiquitination sites discovers the VLI patch-containing bipartite NLS as the putative UBE2O recognition sequence
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UBE2O is an E2/E3 hybrid enzyme and exhibits both the E2 and E3 activities. UBE2O performs monoubiquitination, multi-monoubiquitination, and polyubiquitination of different substrates, mechanisms, overview. A consensus sequence analysis of the UBE2O-mediated ubiquitination sites discovers the VLI patch-containing bipartite NLS as the putative UBE2O recognition sequence
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beta-lactoglobulin and reduced carboxymethylated bovine serum albumin rcmBSA are not conjugates
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