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show all sequences of 2.3.2.B8

Identification of determinants in E2 ubiquitin-conjugating enzymes required for hect E3 ubiquitin-protein ligase interaction

Nuber, U.; Scheffner, M.; J. Biol. Chem. 274, 7576-7582 (1999)

Data extracted from this reference:

Cloned(Commentary)
Commentary
Organism
-
Homo sapiens
-
Mus musculus
Engineering
Amino acid exchange
Commentary
Organism
additional information
generation of chimeric E2 enzymes consisting of different parts of human UbcH5 and murine UbcM3. Chimera consist of the N-terminal 62 amino acids of UbcH5 fused to the C-terminal 85 amino acids of UbcM3 and of the N-terminal 108 amino acids of UbcM3 fused to the C-terminal 85 amino acids of UbcH5, respectively. The ability to interact with E3 enzyme E6-AP maps to the C-terminal 85 amino acids of UbcH5 and particularly to a phenylalanine residue at position 62 of UbcH5 that is conserved among the members of the UBC4/UBC5 subfamily but is not present in any of the other known E2 enzymes
Homo sapiens
additional information
generation of chimeric E2 enzymes consisting of different parts of human UbcH5 and murine UbcM3. Chimera consist of the N-terminal 62 amino acids of UbcH5 fused to the C-terminal 85 amino acids of UbcM3 and of the N-terminal 108 amino acids of UbcM3 fused to the C-terminal 85 amino acids of UbcH5, respectively. The ability to interact with E3 enzyme E6-AP maps to the C-terminal 85 amino acids of UbcH5
Mus musculus
Organism
Organism
Primary Accession No. (UniProt)
Commentary
Textmining
Homo sapiens
P51668
isoform UbcH5
-
Mus musculus
P52482
isoform UbcM3
-
Substrates and Products (Substrate)
Substrates
Commentary Substrates
Literature (Substrates)
Organism
Products
Commentary (Products)
Literature (Products)
Organism (Products)
Reversibility
[ubiquitin-carrier protein UbcH5]-S-ubiquitinyl-L-cysteine + [HECT-E3-ubiquitin-carrier protein E6-AP]-L-cysteine
a region of isoform UbcH5 encompassing the catalytic site cysteine residue is critical for its ability to interact with E3 enzymes E6-AP and RSP5. Of particular importance is a phenylalanine residue at position 62 of UbcH5 that is conserved among the members of the UBC4/UBC5 subfamily but is not present in any of the other known E2s
651978
Homo sapiens
[ubiquitin-carrier protein UbcH5]-L-cysteine + [HECT-E3-ubiquitin-carrier protein E6-AP]-S-ubiquitinyl-L-cysteine
-
-
-
-
[ubiquitin-carrier protein UbcH5]-S-ubiquitinyl-L-cysteine + [HECT-E3-ubiquitin-carrier protein Rsp5]-L-cysteine
a region of isoform UbcH5 encompassing the catalytic site cysteine residue is critical for its ability to interact with E3 enzymes E6-AP and RSP5. Of particular importance is a phenylalanine residue at position 62 of UbcH5 that is conserved among the members of the UBC4/UBC5 subfamily but is not present in any of the other known E2s
651978
Homo sapiens
[ubiquitin-carrier protein UbcH5]-L-cysteine + [HECT-E3-ubiquitin-carrier protein Rsp5]-S-ubiquitinyl-L-cysteine
-
-
-
-
Cloned(Commentary) (protein specific)
Commentary
Organism
-
Homo sapiens
-
Mus musculus
Engineering (protein specific)
Amino acid exchange
Commentary
Organism
additional information
generation of chimeric E2 enzymes consisting of different parts of human UbcH5 and murine UbcM3. Chimera consist of the N-terminal 62 amino acids of UbcH5 fused to the C-terminal 85 amino acids of UbcM3 and of the N-terminal 108 amino acids of UbcM3 fused to the C-terminal 85 amino acids of UbcH5, respectively. The ability to interact with E3 enzyme E6-AP maps to the C-terminal 85 amino acids of UbcH5 and particularly to a phenylalanine residue at position 62 of UbcH5 that is conserved among the members of the UBC4/UBC5 subfamily but is not present in any of the other known E2 enzymes
Homo sapiens
additional information
generation of chimeric E2 enzymes consisting of different parts of human UbcH5 and murine UbcM3. Chimera consist of the N-terminal 62 amino acids of UbcH5 fused to the C-terminal 85 amino acids of UbcM3 and of the N-terminal 108 amino acids of UbcM3 fused to the C-terminal 85 amino acids of UbcH5, respectively. The ability to interact with E3 enzyme E6-AP maps to the C-terminal 85 amino acids of UbcH5
Mus musculus
Substrates and Products (Substrate) (protein specific)
Substrates
Commentary Substrates
Literature (Substrates)
Organism
Products
Commentary (Products)
Literature (Products)
Organism (Products)
Reversibility
[ubiquitin-carrier protein UbcH5]-S-ubiquitinyl-L-cysteine + [HECT-E3-ubiquitin-carrier protein E6-AP]-L-cysteine
a region of isoform UbcH5 encompassing the catalytic site cysteine residue is critical for its ability to interact with E3 enzymes E6-AP and RSP5. Of particular importance is a phenylalanine residue at position 62 of UbcH5 that is conserved among the members of the UBC4/UBC5 subfamily but is not present in any of the other known E2s
651978
Homo sapiens
[ubiquitin-carrier protein UbcH5]-L-cysteine + [HECT-E3-ubiquitin-carrier protein E6-AP]-S-ubiquitinyl-L-cysteine
-
-
-
-
[ubiquitin-carrier protein UbcH5]-S-ubiquitinyl-L-cysteine + [HECT-E3-ubiquitin-carrier protein Rsp5]-L-cysteine
a region of isoform UbcH5 encompassing the catalytic site cysteine residue is critical for its ability to interact with E3 enzymes E6-AP and RSP5. Of particular importance is a phenylalanine residue at position 62 of UbcH5 that is conserved among the members of the UBC4/UBC5 subfamily but is not present in any of the other known E2s
651978
Homo sapiens
[ubiquitin-carrier protein UbcH5]-L-cysteine + [HECT-E3-ubiquitin-carrier protein Rsp5]-S-ubiquitinyl-L-cysteine
-
-
-
-
Other publictions for EC 2.3.2.B8
No.
1st author
Pub Med
title
organims
journal
volume
pages
year
Activating Compound
Application
Cloned(Commentary)
Crystallization (Commentary)
Engineering
General Stability
Inhibitors
KM Value [mM]
Localization
Metals/Ions
Molecular Weight [Da]
Natural Substrates/ Products (Substrates)
Organic Solvent Stability
Organism
Oxidation Stability
Posttranslational Modification
Purification (Commentary)
Reaction
Renatured (Commentary)
Source Tissue
Specific Activity [micromol/min/mg]
Storage Stability
Substrates and Products (Substrate)
Subunits
Temperature Optimum [°C]
Temperature Range [°C]
Temperature Stability [°C]
Turnover Number [1/s]
pH Optimum
pH Range
pH Stability
Cofactor
Ki Value [mM]
pI Value
IC50 Value
Activating Compound (protein specific)
Application (protein specific)
Cloned(Commentary) (protein specific)
Cofactor (protein specific)
Crystallization (Commentary) (protein specific)
Engineering (protein specific)
General Stability (protein specific)
IC50 Value (protein specific)
Inhibitors (protein specific)
Ki Value [mM] (protein specific)
KM Value [mM] (protein specific)
Localization (protein specific)
Metals/Ions (protein specific)
Molecular Weight [Da] (protein specific)
Natural Substrates/ Products (Substrates) (protein specific)
Organic Solvent Stability (protein specific)
Oxidation Stability (protein specific)
Posttranslational Modification (protein specific)
Purification (Commentary) (protein specific)
Renatured (Commentary) (protein specific)
Source Tissue (protein specific)
Specific Activity [micromol/min/mg] (protein specific)
Storage Stability (protein specific)
Substrates and Products (Substrate) (protein specific)
Subunits (protein specific)
Temperature Optimum [°C] (protein specific)
Temperature Range [°C] (protein specific)
Temperature Stability [°C] (protein specific)
Turnover Number [1/s] (protein specific)
pH Optimum (protein specific)
pH Range (protein specific)
pH Stability (protein specific)
pI Value (protein specific)
Expression
General Information
General Information (protein specific)
Expression (protein specific)
KCat/KM [mM/s]
KCat/KM [mM/s] (protein specific)
736486
Riling
Itch WW domains inhibit its E3 ...
Mus musculus
J. Biol. Chem.
290
23875-23887
2015
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736640
Banka
RING E3-catalyzed E2 self-ubiq ...
Homo sapiens
J. Mol. Biol.
427
2290-2304
2015
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736634
Schumacher
The N-terminal extension of UB ...
Homo sapiens
J. Mol. Biol.
425
4099-4111
2013
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725971
Kamadurai
Insights into ubiquitin transf ...
Homo sapiens
Mol. Cell.
36
1095-1102
2009
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1
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651978
Nuber
Identification of determinants ...
Homo sapiens, Mus musculus
J. Biol. Chem.
274
7576-7582
1999
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