Any feedback?
Please rate this page
(enzyme.php)
(0/150)

BRENDA support

BRENDA Home
show all | hide all No of entries

Information on EC 2.3.2.27 - RING-type E3 ubiquitin transferase and Organism(s) Caenorhabditis elegans

for references in articles please use BRENDA:EC2.3.2.27
Please wait a moment until all data is loaded. This message will disappear when all data is loaded.
EC Tree
     2 Transferases
         2.3 Acyltransferases
             2.3.2 Aminoacyltransferases
                2.3.2.27 RING-type E3 ubiquitin transferase
IUBMB Comments
RING E3 ubiquitin transferases serve as mediators bringing the ubiquitin-charged E2 ubiquitin-conjugating enzyme (EC 2.3.2.23) and an acceptor protein together to enable the direct transfer of ubiquitin through the formation of an isopeptide bond between the C-terminal glycine residue of ubiquitin and the epsilon-amino group of an L-lysine residue of the acceptor protein. Unlike EC 2.3.2.26, HECT-type E3 ubiquitin transferase, the RING-E3 domain does not form a catalytic thioester intermediate with ubiquitin. Many members of the RING-type E3 ubiquitin transferase family are not able to bind a substrate directly, and form a complex with a cullin scaffold protein and a substrate recognition module (the complexes are named CRL for Cullin-RING-Ligase). In these complexes, the RING-type E3 ubiquitin transferase provides an additional function, mediating the transfer of a NEDD8 protein from a dedicated E2 carrier to the cullin protein (see EC 2.3.2.32, cullin-RING-type E3 NEDD8 transferase). cf. EC 2.3.2.31, RBR-type E3 ubiquitin transferase.
Specify your search results
Select one or more organisms in this record: ?
This record set is specific for:
Caenorhabditis elegans
Show additional data
Do not include text mining results
Include (text mining) results
Include results (AMENDA + additional results, but less precise)
Word Map
The taxonomic range for the selected organisms is: Caenorhabditis elegans
The enzyme appears in selected viruses and cellular organisms
Reaction Schemes
[E2 ubiquitin-conjugating enzyme]-S-ubiquitinyl-L-cysteine
+
[acceptor protein]-L-lysine
=
[E2 ubiquitin-conjugating enzyme]-L-cysteine
+
[acceptor protein]-N6-ubiquitinyl-L-lysine
Synonyms
brca1, parkin, e3 ubiquitin ligase, e3 ligase, c-cbl, ciap2, trim5alpha, rnf43, trim25, trim5, more
SYNONYM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
PATHWAY SOURCE
PATHWAYS
-
-
SYSTEMATIC NAME
IUBMB Comments
[E2 ubiquitin-conjugating enzyme]-S-ubiquitinyl-L-cysteine:[acceptor protein] ubiquitin transferase (isopeptide bond-forming; RING-type)
RING E3 ubiquitin transferases serve as mediators bringing the ubiquitin-charged E2 ubiquitin-conjugating enzyme (EC 2.3.2.23) and an acceptor protein together to enable the direct transfer of ubiquitin through the formation of an isopeptide bond between the C-terminal glycine residue of ubiquitin and the epsilon-amino group of an L-lysine residue of the acceptor protein. Unlike EC 2.3.2.26, HECT-type E3 ubiquitin transferase, the RING-E3 domain does not form a catalytic thioester intermediate with ubiquitin. Many members of the RING-type E3 ubiquitin transferase family are not able to bind a substrate directly, and form a complex with a cullin scaffold protein and a substrate recognition module (the complexes are named CRL for Cullin-RING-Ligase). In these complexes, the RING-type E3 ubiquitin transferase provides an additional function, mediating the transfer of a NEDD8 protein from a dedicated E2 carrier to the cullin protein (see EC 2.3.2.32, cullin-RING-type E3 NEDD8 transferase). cf. EC 2.3.2.31, RBR-type E3 ubiquitin transferase.
ORGANISM
COMMENTARY hide
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
isoform Ufd-2
UniProt
Manually annotated by BRENDA team
GENERAL INFORMATION
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
physiological function
UFD-2 is a mediator of DNA-damage-induced apoptosis. After initiation of homologous recombination by RAD-51, UFD-2 forms foci that contain substrate-processivity factors including the ubiquitin-selective segregase CDC-48 (p97), the deubiquitination enzyme ATX-3 (Ataxin-3) and the proteasome. In the absence of UFD-2, RAD-51 foci persist, and DNA damage-induced apoptosis is prevented. UFD-2 foci are retained until recombination intermediates are removed by the Holliday-junction-processing enzymes GEN-1, MUS-81 or XPF-1. Formation of UFD-2 foci also requires proapoptotic CEP-1 (p53) signaling
UNIPROT
ENTRY NAME
ORGANISM
NO. OF AA
NO. OF TRANSM. HELICES
MOLECULAR WEIGHT[Da]
SOURCE
SEQUENCE
LOCALIZATION PREDICTION?
UBE4_CAEEL
984
0
113801
Swiss-Prot
other Location (Reliability: 1)
BRE1_CAEEL
837
0
97444
Swiss-Prot
other Location (Reliability: 2)
HRD1_CAEEL
610
6
66814
Swiss-Prot
Secretory Pathway (Reliability: 4)
MKRN_CAEEL
413
0
48090
Swiss-Prot
other Location (Reliability: 1)
LTN1_CAEEL
1446
0
165403
Swiss-Prot
Mitochondrion (Reliability: 4)
RLE1_CAEEL
952
0
104766
Swiss-Prot
other Location (Reliability: 2)
TRI23_CAEEL
539
0
60682
Swiss-Prot
other Location (Reliability: 1)
PRP19_CAEEL
492
0
53208
Swiss-Prot
other Location (Reliability: 1)
PPIL2_CAEEL
523
0
58534
Swiss-Prot
other Location (Reliability: 1)
RNF5_CAEEL
235
2
24915
Swiss-Prot
other Location (Reliability: 1)
BARD1_CAEEL
702
0
78804
Swiss-Prot
other Location (Reliability: 2)
RING2_CAEEL
2476
0
276431
Swiss-Prot
other Location (Reliability: 1)
SIAH1_CAEEL
419
0
45804
Swiss-Prot
other Location (Reliability: 1)
TRUL_CAEEL
451
0
51444
Swiss-Prot
other Location (Reliability: 2)
BRCA1_CAEEL
612
0
69718
Swiss-Prot
other Location (Reliability: 2)
RN113_CAEEL
384
0
43428
Swiss-Prot
other Location (Reliability: 2)
UBR1_CAEEL
2058
0
232816
Swiss-Prot
other Location (Reliability: 4)
Q95ZR5_CAEEL
565
0
64215
TrEMBL
Mitochondrion (Reliability: 3)
Q9XWM0_CAEEL
283
3
32711
TrEMBL
other Location (Reliability: 2)
Q6ABG8_CAEEL
523
0
59805
TrEMBL
Mitochondrion (Reliability: 3)
A0A5S9MML0_CAEEL
2041
0
233913
TrEMBL
other Location (Reliability: 2)
A0A131MD51_CAEEL
218
0
23008
TrEMBL
other Location (Reliability: 1)
G5ECY6_CAEEL
266
0
31089
TrEMBL
other Location (Reliability: 1)
A0A5K1ICF1_CAEEL
927
0
102920
TrEMBL
other Location (Reliability: 1)
Q18782_CAEEL
925
0
102685
TrEMBL
other Location (Reliability: 1)
Q19019_CAEEL
582
0
66070
TrEMBL
Mitochondrion (Reliability: 3)
Q17911_CAEEL
529
0
59446
TrEMBL
other Location (Reliability: 3)
O17719_CAEEL
228
0
25427
TrEMBL
other Location (Reliability: 2)
Q9N3D1_CAEEL
304
0
33447
TrEMBL
other Location (Reliability: 1)
REF.
AUTHORS
TITLE
JOURNAL
VOL.
PAGES
YEAR
ORGANISM (UNIPROT)
PUBMED ID
SOURCE
Ackermann, L.; Schell, M.; Pokrzywa, W.; Kevei, E.; Gartner, A.; Schumacher, B.; Hoppe, T.
E4 ligase-specific ubiquitination hubs coordinate DNA double-strand-break repair and apoptosis
Nat. Struct. Mol. Biol.
23
995-1002
2016
Caenorhabditis elegans (Q09349), Caenorhabditis elegans
Manually annotated by BRENDA team