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Information on EC 2.3.2.23 - E2 ubiquitin-conjugating enzyme and Organism(s) Mus musculus and UniProt Accession Q9Z1K5

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EC Tree
     2 Transferases
         2.3 Acyltransferases
             2.3.2 Aminoacyltransferases
                2.3.2.23 E2 ubiquitin-conjugating enzyme
IUBMB Comments
The E2 ubiquitin-conjugating enzyme acquires the activated ubquitin from the E1 ubiquitin-activating enzyme (EC 6.2.1.45) and binds it via a transthioesterification reaction to itself. In the human enzyme the catalytic center is located at Cys-87 where ubiquitin is bound via its C-terminal glycine in a thioester linkage.
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This record set is specific for:
Mus musculus
UNIPROT: Q9Z1K5
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The taxonomic range for the selected organisms is: Mus musculus
The enzyme appears in selected viruses and cellular organisms
Reaction Schemes
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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-[E1 ubiquitin-activating enzyme]-L-cysteine
+
[E2 ubiquitin-conjugating enzyme]-L-cysteine
=
[E1 ubiquitin-activating enzyme]-L-cysteine
+
S-ubiquitinyl-[E2 ubiquitin-conjugating enzyme]-L-cysteine
Synonyms
ube2c, cdc34, ubc13, ube2t, ubch10, e2 enzyme, ube2s, ubch7, e2 ubiquitin-conjugating enzyme, ube2l3, more
SYNONYM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
E2 Ub-conjugating enzyme
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PATHWAY SOURCE
PATHWAYS
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SYSTEMATIC NAME
IUBMB Comments
S-ubiquitinyl-[E1 ubiquitin-activating enzyme]-L-cysteine:[E2 ubiquitin-conjugating enzyme] ubiquitinyl transferase
The E2 ubiquitin-conjugating enzyme acquires the activated ubquitin from the E1 ubiquitin-activating enzyme (EC 6.2.1.45) and binds it via a transthioesterification reaction to itself. In the human enzyme the catalytic center is located at Cys-87 where ubiquitin is bound via its C-terminal glycine in a thioester linkage.
SUBSTRATE
PRODUCT                       
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate) hide
LITERATURE
(Substrate)
COMMENTARY
(Product) hide
LITERATURE
(Product)
Reversibility
r=reversible
ir=irreversible
?=not specified
[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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-
-
?
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
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-
-
?
NATURAL SUBSTRATE
NATURAL PRODUCT
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
-
-
-
?
ACTIVATING COMPOUND
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
additional information
Derlin2 interacts with UBC6e in the complex involved in the regulation of ERAD enhancers. Derlin2 levels do not change in UBC6e-/- cells transduced with any of the UBC6e mutants, suggesting that it is not a substrate regulated by UBC6e, but is a member of a UBC6e complex
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ORGANISM
COMMENTARY hide
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
isoform UbcH7
UniProt
Manually annotated by BRENDA team
SOURCE TISSUE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
SOURCE
LOCALIZATION
ORGANISM
UNIPROT
COMMENTARY hide
GeneOntology No.
LITERATURE
SOURCE
UBC6e localizes to the ER via its tail-anchor, functional UBC6e requires its precise location in the endoplasmic reticulum to form a supramolecular complex with Derlin2
Manually annotated by BRENDA team
GENERAL INFORMATION
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
malfunction
ablation of UBC6e causes upregulation of active ERAD enhancers and so increases clearance not only of terminally misfolded substrates, but also of wild-type glycoproteins that fold comparatively slowly in vitro and in vivo. The absence of UBC6e increases the levels of ERAD enhancers with a corresponding increase in the rate of clearance of misfolded and/or incompletely folded substrates. UBC6e-/- MEFs show accelerated mannose trimming and premature substrate release from CNX, initiated by ER mannosidase-dependent eviction of substrate from the CNX cycle. Finally, by deletion of UBC6e, accelerated degradation is observed in tissue culture and in vivo, not only for canonical ERAD substrates, but also for folding intermediates of proteins that fold slowly, such as tyrosinase. The UBC6e loss-of-function mutation thus produces a gain-of-function with respect to ERAD activity, overview. Increased degradation of tyrosinase in UBC6e-/- cells and reduced skin tyrosinase levels in UBC6e-/- mice
metabolism
the enzyme UbeC6 is involved in the endoplasmic reticulum (ER) associated degradation (ERAD)
physiological function
UNIPROT
ENTRY NAME
ORGANISM
NO. OF AA
NO. OF TRANSM. HELICES
MOLECULAR WEIGHT[Da]
SOURCE
SEQUENCE
LOCALIZATION PREDICTION?
ARI1_MOUSE
555
0
64017
Swiss-Prot
other Location (Reliability: 3)
SUBUNIT
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
additional information
UBC6e exists in at least two different configurations: as an apparent monomer and as part of a complex
PROTEIN VARIANTS
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
additional information
generation of UbeC6 deletion mice, phenotype, detailed overview. Generation of Derlin2-/- mice showing that not only ERAD enhancers but also UBC6e itself are upregulated
CLONED (Commentary)
ORGANISM
UNIPROT
LITERATURE
expresion in Escherichia coli
REF.
AUTHORS
TITLE
JOURNAL
VOL.
PAGES
YEAR
ORGANISM (UNIPROT)
PUBMED ID
SOURCE
Carvalho, A.F.; Pinto, M.P.; Grou, C.P.; Vitorino, R.; Domingues, P.; Yamao, F.; Sa-Miranda, C.; Azevedo, J.E.
High-yield expression in Escherichia coli and purification ofmouse ubiquitin-activating enzyme E1
Mol. Biotechnol.
51
254-261
2012
Mus musculus (Q9Z1K5)
Manually annotated by BRENDA team
Koenig, P.A.; Nicholls, P.K.; Schmidt, F.I.; Hagiwara, M.; Maruyama, T.; Frydman, G.H.; Watson, N.; Page, D.C.; Ploegh, H.L.
The E2 ubiquitin-conjugating enzyme UBE2J1 is required for spermiogenesis in mice
J. Biol. Chem.
289
34490-34502
2014
Mus musculus (Q9JJZ4)
Manually annotated by BRENDA team
Hagiwara, M.; Ling, J.; Koenig, P.A.; Ploegh, H.L.
Posttranscriptional regulation of glycoprotein quality control in the endoplasmic reticulum is controlled by the E2 Ub-conjugating enzyme UBC6e
Mol. Cell
63
753-767
2016
Mus musculus (Q9JJZ4)
Manually annotated by BRENDA team