Information on EC 2.3.2.23 - E2 ubiquitin-conjugating enzyme

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The expected taxonomic range for this enzyme is: Eukaryota, Bacteria

EC NUMBER
COMMENTARY hide
2.3.2.23
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RECOMMENDED NAME
GeneOntology No.
E2 ubiquitin-conjugating enzyme
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REACTION
REACTION DIAGRAM
COMMENTARY hide
ORGANISM
UNIPROT
LITERATURE
S-ubiquitinyl-[E1 ubiquitin-activating enzyme]-L-cysteine + [E2 ubiquitin-conjugating enzyme]-L-cysteine = [E1 ubiquitin-activating enzyme]-L-cysteine + S-ubiquitinyl-[E2 ubiquitin-conjugating enzyme]-L-cysteine
show the reaction diagram
REACTION TYPE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
transthioesterification
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PATHWAY
BRENDA Link
KEGG Link
MetaCyc Link
protein ubiquitylation
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SYSTEMATIC NAME
IUBMB Comments
S-ubiquitinyl-[E1 ubiquitin-activating enzyme]-L-cysteine:[E2 ubiquitin-conjugating enzyme] ubiquitinyl transferase
The E2 ubiquitin-conjugating enzyme acquires the activated ubquitin from the E1 ubiquitin-activating enzyme (EC 6.2.1.45) and binds it via a transthioesterification reaction to itself. In the human enzyme the catalytic center is located at Cys-87 where ubiquitin is bound via its C-terminal glycine in a thioester linkage.
ORGANISM
COMMENTARY hide
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
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Manually annotated by BRENDA team
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UniProt
Manually annotated by BRENDA team
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Manually annotated by BRENDA team
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Manually annotated by BRENDA team
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UniProt
Manually annotated by BRENDA team
GENERAL INFORMATION
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
malfunction
physiological function
SUBSTRATE
PRODUCT                       
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate) hide
LITERATURE
(Substrate)
COMMENTARY
(Product) hide
LITERATURE
(Product)
Reversibility
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
show the reaction diagram
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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
show the reaction diagram
S-ubiquitinyl-[Uba1]-L-cysteine + [Ubc5a]-L-cysteine
[Uba1]-L-cysteine + S-ubiquitinyl-[Ubc5a]-L-cysteine
show the reaction diagram
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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
show the reaction diagram
binding of Ubc4 to the E1–ubiquitin 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
show the reaction diagram
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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
show the reaction diagram
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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
show the reaction diagram
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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
show the reaction diagram
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
show the reaction diagram
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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
show the reaction diagram
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
show the reaction diagram
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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
show the reaction diagram
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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
show the reaction diagram
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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
show the reaction diagram
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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
show the reaction diagram
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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
show the reaction diagram
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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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?
additional information
?
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NATURAL SUBSTRATES
NATURAL PRODUCTS
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate) hide
LITERATURE
(Substrate)
COMMENTARY
(Product) hide
LITERATURE
(Product)
REVERSIBILITY
r=reversible
ir=irreversible
?=not specified
S-ubiquitinyl-[E1 ubiquitin-activating enzyme]-L-cysteine + [E2 ubiquitin-conjugating enzyme]-L-cysteine
[E1 ubiquitin-activating enzyme]-L-cysteine + S-ubiquitinyl-[E2 ubiquitin-conjugating enzyme]-L-cysteine
show the reaction diagram
KM VALUE [mM]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
0.0019
[ubiquitin carrier protein Ubc4]-L-cysteine
pH 7.5, 25°C
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0.000073 - 0.000135
[ubiquitin-carrier-protein Ubc2b]-L-cysteine
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TURNOVER NUMBER [1/s]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
0.072
[ubiquitin carrier protein Ubc4]-L-cysteine
Homo sapiens
P62837
pH 7.5, 25°C
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0.01 - 3.4
[ubiquitin-carrier-protein Ubc2b]-L-cysteine
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pH OPTIMUM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
7.5
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assay at, polyubiquitination
TEMPERATURE OPTIMUM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
37
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assay at, polyubiquitination
SOURCE TISSUE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
SOURCE
colon carcinoma cell
Manually annotated by BRENDA team
additional information
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most E2 enzymes have been identified in a wide variety of tissues and cell types
Manually annotated by BRENDA team
LOCALIZATION
ORGANISM
UNIPROT
COMMENTARY hide
GeneOntology No.
LITERATURE
SOURCE
additional information
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many E2 enzymes are found both in the nucleus and in the cytoplasm. Some E2 enzymes are exclusively restructed to specific compartments
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Manually annotated by BRENDA team
PDB
SCOP
CATH
ORGANISM
UNIPROT
Saccharomyces cerevisiae (strain ATCC 204508 / S288c)
Saccharomyces cerevisiae (strain ATCC 204508 / S288c)
Saccharomyces cerevisiae (strain ATCC 204508 / S288c)
Saccharomyces cerevisiae (strain ATCC 204508 / S288c)
Saccharomyces cerevisiae (strain ATCC 204508 / S288c)
Saccharomyces cerevisiae (strain ATCC 204508 / S288c)
Saccharomyces cerevisiae (strain ATCC 204508 / S288c)
Saccharomyces cerevisiae (strain ATCC 204508 / S288c)
Saccharomyces cerevisiae (strain ATCC 204508 / S288c)
Saccharomyces cerevisiae (strain ATCC 204508 / S288c)
Saccharomyces cerevisiae (strain ATCC 204508 / S288c)
Saccharomyces cerevisiae (strain ATCC 204508 / S288c)
Saccharomyces cerevisiae (strain ATCC 204508 / S288c)
Saccharomyces cerevisiae (strain ATCC 204508 / S288c)
Saccharomyces cerevisiae (strain ATCC 204508 / S288c)
Saccharomyces cerevisiae (strain ATCC 204508 / S288c)
MOLECULAR WEIGHT
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
16500
x * 16500, calculated
18000
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2 * 18000, single band on SDS-PAGE, indicating a dimeric form. Gel filtration results in an estimated molecular weight of 42 kDa
18400
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2 * 18400, SDS-PAGE
30000
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x * 30000, SDS-PAGE
42000
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gel filtration results in an estimated molecular weight of 42 kDa
SUBUNITS
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
homodimer
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2 * 18400, SDS-PAGE
additional information
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isoformUbc2 interacts with disease-related protein SGT1
POSTTRANSLATIONAL MODIFICATION
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
additional information
Crystallization/COMMENTARY
ORGANISM
UNIPROT
LITERATURE
recombinant enzyme, N-terminally His-tagged, subcloned in Escherichia coli BL21(DE2), via pET28 vector, purified using Ni-NTA column and HiLoad 16/60 Superdex 75 gel filtration column, diffracted X-rays to 1.7 A. The crystal belongs to space group C2
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using 20% (w/v) PEG 3350, 0.2 M sodium acetate, and 0.1 M Bis-Tris, pH 6.5
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2.9 A crystal structure of the ubiquitin ligase CHIP U-box domain complexed with UbcH5a. CHIP binds to UbcH5 and Ubc13 through similar specificity determinants located on the long loops and central helix of the CHIP U-box, and on the N-terminal helix and loops L4 and L7 of its cognate E2 enzymes including a key S-P-A motif. The determinants make different relative contributions to the overall interactions between CHIP and the two E2 enzymes. CHIP undergoes auto-ubiquitination by UbcH5
crystal structures of the C-terminal ubiquitin fold domain from yeast Uba2 alone and in complex with E2 enzyme Ubc9. Uba2 undergoes remarkable conformational changes during the reaction. The structure of the Uba2 domain-Ubc9 complex reveals interactions unique to Sumo E1 and E2. Comparison with a previous Ubc9-E3 complex structure demonstrates overlap between Uba2 and E3 binding sites on Ubc9, indicating that loading with Sumo and E3-catalyzed transfer to substrates are strictly separate steps
mutant C105S/C146S in complex with the soluble domain of peroxisomal membrane protein Pex22. Structure shows a narrowing of the active site cleft, caused by loss of the disulfide bond
Purification/COMMENTARY
ORGANISM
UNIPROT
LITERATURE
Ni-NTA column chromatography and Superdex 75 gel filtration
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recombinant enzyme, N-terminally His-tagged, subcloned in Escherichia coli BL21(DE2), via pET28 vector, purified using Ni-NTA column and HiLoad 16/60 Superdex 75 gel filtration column, purity 95% after two steps
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recombinant protein, Ni-NTA column
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Cloned/COMMENTARY
ORGANISM
UNIPROT
LITERATURE
a fragment of the enzyme is cloned into a virus-induced genesilencing vector based on the geminivirus tomato mottlevirus
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expresion in Escherichia coli
expressed and transformed into Escherichia coli (BL-21 DE3) using pET22 vector in frame to a C-terminal His6 tag
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expressed in HEK-293T, HeLa, or U2OS cells
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expression in baculoviral system
expression in Escherichia coli
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subcloned in Escherichia coli BL21(DE2), via pET28 vector, N-terminally His-tagged
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EXPRESSION
ORGANISM
UNIPROT
LITERATURE
isoform Ubc1 expression is not induced by low temperature or wounding
isoform UBC1 mRNA expression is induced by either dehydration, high salinity or by the exogenous abscisic acid
the expression of the enzyme is significantly up-regulated after cold-treatment at 4°C lasting for 4, 6, and 8 h
the majority of E2s are expressed ubiquitously
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ENGINEERING
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
C136F
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mutation results in constitutive binding of UbcM2 to transcription factor Nrf2 and an increased half-life of the transcription factor in vivo
C93S
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sumoylatzion-defective mutant
DELTA946
truncation of the Uba3 carboxyl-terminal beta-grasp domain, no effect on cognate Ubc12 thiolester formation
K323R
mutation in site of auto-FAT10ylation. Mutation does not abolish auto-FAT10ylation of USE1, but every other lysine can instead be modified with FAT10
K86V
during transfer of ubiquitin to the final substrate or E3 ligase, reaction of EC 2.3.2.27, mutant shows increased polyubiquitin chain building activity with ubiquitin mutant K48R
N80Q
during transfer of ubiquitin to the final substrate or E3 ligase, reaction of EC 2.3.2.27, mutant shows increased polyubiquitin chain building activity with ubiquitin mutant K48R
P79A
during transfer of ubiquitin to the final substrate or E3 ligase, reaction of EC 2.3.2.27, mutant shows a much reduced capacity to ubiquitylate RING-E3 enzyme RNF25
R13A/K14A
mutations in Ubc9 disrupt the interaction with SUMO-1 but do not completely abolish the interaction with E1 enzyme. Mutant displays a significantly reduced efficiency in the transfer of SUMO-1 from E1 to Ubc9, its ability to recognize substrate and transfer SUMO-1 from Ubc9 to the target protein is unaffected
R17A/K18A
mutations in Ubc9 disrupt the interaction with SUMO-1 but do not completely abolish the interaction with E1 enzyme. Mutant displays a significantly reduced efficiency in the transfer of SUMO-1 from E1 to Ubc9, its ability to recognize substrate and transfer SUMO-1 from Ubc9 to the target protein is unaffected
R94Q/L98M
during transfer of ubiquitin to the final substrate or E3 ligase, reaction of EC 2.3.2.27, mutant shows increased polyubiquitin chain building activity with ubiquitin mutant K48R
C105S/C146S
mutation of the residues forming an intramolecular disulfide bond. Mutation does not disturb the secondary structure of the protein but does reduce the in vitro activity of isoform Pex4
K118R
residue Lys118 is required for Ubc7 activity. Mutant is very poor in assembly of polyubiquitin chains. Lys118 is both essential and sufficient for Doa10-mediated degradation of substrates
APPLICATION
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
drug development
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UbcA1 shows antitumor properties, a potential anticancer drug candidate
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