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Information on EC 2.3.2.23 - E2 ubiquitin-conjugating enzyme and Organism(s) Danio rerio

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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:
Danio rerio
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Word Map
The taxonomic range for the selected organisms is: Danio rerio
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.
ORGANISM
COMMENTARY hide
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
-
UniProt
Manually annotated by BRENDA team
UNIPROT
ENTRY NAME
ORGANISM
NO. OF AA
NO. OF TRANSM. HELICES
MOLECULAR WEIGHT[Da]
SOURCE
SEQUENCE
LOCALIZATION PREDICTION?
UBE2S_DANRE
221
0
24149
Swiss-Prot
other Location (Reliability: 2)
UBE2T_DANRE
194
0
21891
Swiss-Prot
other Location (Reliability: 5)
UBE2Z_DANRE
328
0
36451
Swiss-Prot
other Location (Reliability: 5)
UB2WA_DANRE
151
0
17399
Swiss-Prot
other Location (Reliability: 2)
UB2WB_DANRE
151
0
17307
Swiss-Prot
other Location (Reliability: 2)
A0A2R8QGJ9_DANRE
208
0
23496
TrEMBL
other Location (Reliability: 2)
F1QWM3_DANRE
176
0
19880
TrEMBL
other Location (Reliability: 2)
Q5PR60_DANRE
200
0
22395
TrEMBL
other Location (Reliability: 2)
A0A8M1N066_DANRE
380
0
41288
TrEMBL
other Location (Reliability: 1)
Q5BLA9_DANRE
200
0
22275
TrEMBL
other Location (Reliability: 2)
Q6PC58_DANRE
147
0
16635
TrEMBL
-
CRYSTALLIZATION (Commentary)
ORGANISM
UNIPROT
LITERATURE
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
CLONED (Commentary)
ORGANISM
UNIPROT
LITERATURE
REF.
AUTHORS
TITLE
JOURNAL
VOL.
PAGES
YEAR
ORGANISM (UNIPROT)
PUBMED ID
SOURCE
Xu, Z.; Kohli, E.; Devlin, K.I.; Bold, M.; Nix, J.C.; Misra, S.
Interactions between the quality control ubiquitin ligase CHIP and ubiquitin conjugating enzymes
BMC Struct. Biol.
8
26
2008
Danio rerio (Q6PC58)
Manually annotated by BRENDA team