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Information on EC 2.3.2.26 - HECT-type E3 ubiquitin transferase and Organism(s) Mus musculus

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EC Tree
     2 Transferases
         2.3 Acyltransferases
             2.3.2 Aminoacyltransferases
                2.3.2.26 HECT-type E3 ubiquitin transferase
IUBMB Comments
In the first step the enzyme transfers ubiquitin from the E2 ubiquitin-conjugating enzyme (EC 2.3.2.23) to a cysteine residue in its HECT domain (which is located in the C-terminal region), forming a thioester bond. In a subsequent step the enzyme transfers the ubiquitin to an acceptor protein, resulting in 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. cf. EC 2.3.2.27, RING-type E3 ubiquitin transferase and EC 2.3.2.31, RBR-type E3 ubiquitin transferase.
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This record set is specific for:
Mus musculus
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Word Map
The taxonomic range for the selected organisms is: Mus musculus
The expected taxonomic range for this enzyme is: Eukaryota, Bacteria, Archaea
Reaction Schemes
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[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
nedd4, smurf1, smurf2, huwe1, nedd4l, nedd4-1, e6-ap, ube3c, trp120, trip12, more
SYNONYM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
HECT domain E3 ubiquitin ligase
-
-
HECT-type E3 ligase
-
-
HECT-type ubiquitin E3 ligase
-
-
Itch
-
-
TRIP12
-
-
PATHWAY SOURCE
PATHWAYS
-
-
SYSTEMATIC NAME
IUBMB Comments
[E2 ubiquitin-conjugating enzyme]-S-ubiquitinyl-L-cysteine:[acceptor protein] ubiquitin transferase (isopeptide bond-forming)
In the first step the enzyme transfers ubiquitin from the E2 ubiquitin-conjugating enzyme (EC 2.3.2.23) to a cysteine residue in its HECT domain (which is located in the C-terminal region), forming a thioester bond. In a subsequent step the enzyme transfers the ubiquitin to an acceptor protein, resulting in 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. cf. EC 2.3.2.27, RING-type E3 ubiquitin transferase and EC 2.3.2.31, RBR-type E3 ubiquitin transferase.
SUBSTRATE
PRODUCT                       
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate) hide
LITERATURE
(Substrate)
COMMENTARY
(Product) hide
LITERATURE
(Product)
Reversibility
r=reversible
ir=irreversible
?=not specified
S-ubiquitinyl-[HECT-type E3 ubiquitin transferase]-L-cysteine + [Sox6 protein]-L-lysine
[HECT-type E3 ubiquitin transferase]-L-cysteine + N6-ubiquitinyl-[Sox6 protein]-L-lysine
show the reaction diagram
-
-
-
-
?
[E2 ubiquitin-conjugating enzyme]-S-ubiquitinyl-L-cysteine + [my-opioid receptor MOR1]-L-lysine
[E2 ubiquitin-conjugating enzyme]-L-cysteine + [my-opioid receptor MOR1]-N6-ubiquitinyl-L-lysine
show the reaction diagram
-
-
-
?
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-[HECT-type E3 ubiquitin transferase]-L-cysteine + [Sox6 protein]-L-lysine
[HECT-type E3 ubiquitin transferase]-L-cysteine + N6-ubiquitinyl-[Sox6 protein]-L-lysine
show the reaction diagram
-
-
-
-
?
ORGANISM
COMMENTARY hide
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
LOCALIZATION
ORGANISM
UNIPROT
COMMENTARY hide
GeneOntology No.
LITERATURE
SOURCE
enzyme UBR5 localizes in the nuclei of smooth muscle cells and forms a complex with myocardin in vivo and in vitro
Manually annotated by BRENDA team
GENERAL INFORMATION
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
malfunction
physiological function
UNIPROT
ENTRY NAME
ORGANISM
NO. OF AA
NO. OF TRANSM. HELICES
MOLECULAR WEIGHT[Da]
SOURCE
SEQUENCE
LOCALIZATION PREDICTION?
HERC4_MOUSE
1057
0
118412
Swiss-Prot
other Location (Reliability: 2)
HERC2_MOUSE
4836
0
527456
Swiss-Prot
other Location (Reliability: 2)
WWP1_MOUSE
918
0
104694
Swiss-Prot
other Location (Reliability: 4)
G2E3_MOUSE
716
0
81784
Swiss-Prot
other Location (Reliability: 1)
ITCH_MOUSE
864
0
98994
Swiss-Prot
other Location (Reliability: 2)
HECD1_MOUSE
2618
0
290086
Swiss-Prot
other Location (Reliability: 4)
HECD2_MOUSE
774
0
87773
Swiss-Prot
other Location (Reliability: 2)
HECD3_MOUSE
861
0
97347
Swiss-Prot
Mitochondrion (Reliability: 2)
HECW1_MOUSE
1604
0
179467
Swiss-Prot
Mitochondrion (Reliability: 4)
HECW2_MOUSE
1578
0
176235
Swiss-Prot
Mitochondrion (Reliability: 2)
HUWE1_MOUSE
4377
0
482635
Swiss-Prot
other Location (Reliability: 3)
NEDD4_MOUSE
887
0
102706
Swiss-Prot
other Location (Reliability: 1)
AREL1_MOUSE
823
1
94199
Swiss-Prot
Secretory Pathway (Reliability: 1)
UBR5_MOUSE
2792
0
308352
Swiss-Prot
other Location (Reliability: 1)
WWP2_MOUSE
870
0
98761
Swiss-Prot
Mitochondrion (Reliability: 3)
SMUF1_MOUSE
731
0
83356
Swiss-Prot
Mitochondrion (Reliability: 4)
SMUF2_MOUSE
748
0
86175
Swiss-Prot
Mitochondrion (Reliability: 4)
UBE3A_MOUSE
870
0
99819
Swiss-Prot
other Location (Reliability: 3)
UBE3B_MOUSE
1070
0
122762
Swiss-Prot
Mitochondrion (Reliability: 3)
UBE3C_MOUSE
1083
0
123976
Swiss-Prot
other Location (Reliability: 4)
UBE3D_MOUSE
368
0
40753
Swiss-Prot
other Location (Reliability: 5)
HACE1_MOUSE
909
0
102114
Swiss-Prot
Mitochondrion (Reliability: 5)
NED4L_MOUSE
1004
0
115419
Swiss-Prot
other Location (Reliability: 1)
TRIPC_MOUSE
2025
0
224128
Swiss-Prot
other Location (Reliability: 5)
Q3TXI7_MOUSE
431
0
51060
TrEMBL
other Location (Reliability: 1)
Q5EBQ8_MOUSE
119
0
13283
TrEMBL
other Location (Reliability: 2)
Q3TEQ5_MOUSE
243
1
27696
TrEMBL
Secretory Pathway (Reliability: 1)
Q641N8_MOUSE
875
0
101627
TrEMBL
other Location (Reliability: 3)
Q3TQK9_MOUSE
896
0
103613
TrEMBL
other Location (Reliability: 4)
E9PXB7_MOUSE
835
0
96396
TrEMBL
other Location (Reliability: 5)
A0A0B4J1N9_MOUSE
982
0
106459
TrEMBL
other Location (Reliability: 5)
C6EQH2_MOUSE
4746
0
517328
TrEMBL
other Location (Reliability: 5)
Q3UV52_MOUSE
918
0
104621
TrEMBL
other Location (Reliability: 4)
A0A494BAX0_MOUSE
1004
0
115409
TrEMBL
other Location (Reliability: 1)
A0A0G2JDR9_MOUSE
644
0
74081
TrEMBL
other Location (Reliability: 4)
Q91Z48_MOUSE
149
0
16816
TrEMBL
other Location (Reliability: 2)
Q571M5_MOUSE
876
0
100246
TrEMBL
other Location (Reliability: 2)
Q4JG03_MOUSE
4378
0
482746
TrEMBL
other Location (Reliability: 3)
A0A494B9L5_MOUSE
751
0
87141
TrEMBL
other Location (Reliability: 5)
A0A494BA39_MOUSE
872
0
100906
TrEMBL
other Location (Reliability: 1)
B9EKB3_MOUSE
918
0
104708
TrEMBL
other Location (Reliability: 4)
A0A494B953_MOUSE
956
0
110161
TrEMBL
other Location (Reliability: 1)
S4R2P2_MOUSE
243
0
27783
TrEMBL
Mitochondrion (Reliability: 3)
E9PYU8_MOUSE
757
0
86114
TrEMBL
Mitochondrion (Reliability: 4)
Q3UJU3_MOUSE
824
0
94100
TrEMBL
Mitochondrion (Reliability: 3)
O88380_MOUSE
70
0
8254
TrEMBL
other Location (Reliability: 3)
Q05BY9_MOUSE
499
0
54309
TrEMBL
other Location (Reliability: 4)
Q3T9S4_MOUSE
642
0
70104
TrEMBL
other Location (Reliability: 4)
G3X9H8_MOUSE
855
0
98456
TrEMBL
other Location (Reliability: 5)
D3Z587_MOUSE
138
0
14535
TrEMBL
other Location (Reliability: 4)
Q9D0H0_MOUSE
368
0
40750
TrEMBL
other Location (Reliability: 5)
A0A0G2JG76_MOUSE
178
0
20265
TrEMBL
other Location (Reliability: 3)
Q3TEJ5_MOUSE
494
0
53610
TrEMBL
other Location (Reliability: 4)
I3RSH5_MOUSE
870
0
98761
TrEMBL
Mitochondrion (Reliability: 3)
A0A087WSG4_MOUSE
213
0
22804
TrEMBL
Mitochondrion (Reliability: 3)
E9Q4K9_MOUSE
728
0
83110
TrEMBL
Mitochondrion (Reliability: 4)
Q3UQY6_MOUSE
639
0
68620
TrEMBL
other Location (Reliability: 4)
A0A494BAG2_MOUSE
976
0
112220
TrEMBL
other Location (Reliability: 1)
Q3U5E1_MOUSE
763
0
83552
TrEMBL
other Location (Reliability: 4)
Q8R0U4_MOUSE
399
0
45401
TrEMBL
other Location (Reliability: 5)
A0A494B9F0_MOUSE
912
0
105061
TrEMBL
other Location (Reliability: 1)
B2RSC8_MOUSE
887
0
102706
TrEMBL
other Location (Reliability: 1)
A0A1Y7VJ05_MOUSE
1177
0
131935
TrEMBL
other Location (Reliability: 1)
Q6P289_MOUSE
806
0
92438
TrEMBL
other Location (Reliability: 2)
Q8C5S2_MOUSE
308
0
34794
TrEMBL
other Location (Reliability: 1)
F8WIE5_MOUSE
2610
0
289229
TrEMBL
other Location (Reliability: 4)
Q05CE4_MOUSE
787
0
90083
TrEMBL
other Location (Reliability: 2)
A0A087WNZ7_MOUSE
1992
0
220661
TrEMBL
other Location (Reliability: 5)
A0A494BAE4_MOUSE
527
0
61660
TrEMBL
other Location (Reliability: 5)
A0A087WRV6_MOUSE
830
0
94901
TrEMBL
other Location (Reliability: 3)
A0A1D5RM92_MOUSE
824
0
94158
TrEMBL
Mitochondrion (Reliability: 3)
A2AFQ0_MOUSE
4378
0
482692
TrEMBL
other Location (Reliability: 3)
A0A0G2JEN5_MOUSE
309
0
35353
TrEMBL
other Location (Reliability: 1)
A0A571BDN7_MOUSE
1136
0
127651
TrEMBL
Mitochondrion (Reliability: 5)
PDB
SCOP
CATH
UNIPROT
ORGANISM
MOLECULAR WEIGHT
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
113000
-
x * 113000, SDS-PAGE
200000
-
x * 200000, SDS-PAGE
SUBUNIT
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
EXPRESSION
ORGANISM
UNIPROT
LITERATURE
enzyme expression is increased 3 h after Dox stimulation (0.0005 mM)
-
REF.
AUTHORS
TITLE
JOURNAL
VOL.
PAGES
YEAR
ORGANISM (UNIPROT)
PUBMED ID
SOURCE
Hu, G.; Wang, X.; Saunders, D.; Henderson, M.; Russell, A.; Herring, B.; Zhou, J.
Modulation of myocardin function by the ubiquitin E3 ligase UBR5
J. Biol. Chem.
286
11800-11809
2011
Mus musculus (Q80TP3)
Manually annotated by BRENDA team
Otaki, Y.; Takahashi, H.; Watanabe, T.; Funayama, A.; Netsu, S.; Honda, Y.; Narumi, T.; Kadowaki, S.; Hasegawa, H.; Honda, S.; Arimoto, T.; Shishido, T.; Miyamoto, T.; Kamata, H.; Nakajima, O.; Kubota, I.
HECT-type ubiquitin E3 ligase ITCH interacts with thioredoxin-interacting protein and ameliorates reactive oxygen species-induced cardiotoxicity
J. Am. Heart Assoc.
5
e002485
2016
Mus musculus, Rattus norvegicus
Manually annotated by BRENDA team
An, C.I.; Ganio, E.; Hagiwara, N.
Trip12, a HECT domain E3 ubiquitin ligase, targets Sox6 for proteasomal degradation and affects fiber type-specific gene expression in muscle cells
Skeletal Muscle
3
11
2013
Homo sapiens (Q14669), Mus musculus
Manually annotated by BRENDA team
Dong, S.; Liu, J.; Li, L.; Wang, H.; Ma, H.; Zhao, Y.; Zhao, J.
The HECT ubiquitin E3 ligase Smurf2 degrades my-opioid receptor 1 in the ubiquitin-proteasome system in lung epithelial cells
Am. J. Physiol. Cell Physiol.
316
C632-C640
2019
Mus musculus (A2A5Z6)
Manually annotated by BRENDA team