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Information on EC 2.3.2.23 - E2 ubiquitin-conjugating enzyme and Organism(s) Caenorhabditis elegans

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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:
Caenorhabditis elegans
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Word Map
The taxonomic range for the selected organisms is: Caenorhabditis elegans
The enzyme appears in selected viruses and cellular organisms
Reaction Schemes
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
PATHWAY SOURCE
PATHWAYS
-
-
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
additional information
?
-
ORGANISM
COMMENTARY hide
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
GENERAL INFORMATION
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
physiological function
HECT-E3 ligase ETC-1 ubiquitylates securin IFY-1 and cyclin B1 in the presence of the E2 enzyme UBC-18, which functions in pharyngeal development. UBC-18 plays a distinct role together with ETC-1 in regulating the cytoplasmic level of IFY-1 during meiosis
UNIPROT
ENTRY NAME
ORGANISM
NO. OF AA
NO. OF TRANSM. HELICES
MOLECULAR WEIGHT[Da]
SOURCE
SEQUENCE
LOCALIZATION PREDICTION?
UBC7_CAEEL
164
0
18939
Swiss-Prot
other Location (Reliability: 2)
UBC13_CAEEL
151
0
16902
Swiss-Prot
other Location (Reliability: 4)
UBE2W_CAEEL
152
0
16936
Swiss-Prot
other Location (Reliability: 2)
UBC18_CAEEL
153
0
17653
Swiss-Prot
other Location (Reliability: 2)
UBC1_CAEEL
192
0
21513
Swiss-Prot
other Location (Reliability: 4)
UBC21_CAEEL
214
0
24204
Swiss-Prot
Mitochondrion (Reliability: 5)
UBC25_CAEEL
387
0
44061
Swiss-Prot
other Location (Reliability: 2)
UBC2_CAEEL
147
0
16705
Swiss-Prot
other Location (Reliability: 2)
Q9TZ69_CAEEL
199
0
22291
TrEMBL
other Location (Reliability: 2)
REF.
AUTHORS
TITLE
JOURNAL
VOL.
PAGES
YEAR
ORGANISM (UNIPROT)
PUBMED ID
SOURCE
Wang, R.; Kaul, Z.; Ambardekar, C.; Yamamoto, T.G.; Kavdia, K.; Kodali, K.; High, A.A.; Kitagawa, R.
HECT-E3 ligase ETC-1 regulates securin and cyclin B1 cytoplasmic abundance to promote timely anaphase during meiosis in C. elegans
Development
140
2149-2159
2013
Caenorhabditis elegans (Q21633), Caenorhabditis elegans
Manually annotated by BRENDA team