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Information on EC 2.3.2.B8 - E2:E3 ubiquitin transferase and Organism(s) Mus musculus and UniProt Accession P52482

for references in articles please use BRENDA:EC2.3.2.B8
preliminary BRENDA-supplied EC number
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EC Tree
     2 Transferases
         2.3 Acyltransferases
             2.3.2 Aminoacyltransferases
                2.3.2.B8 E2:E3 ubiquitin transferase
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This record set is specific for:
Mus musculus
UNIPROT: P52482 not found.
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Word Map
The taxonomic range for the selected organisms is: Mus musculus
The enzyme appears in selected viruses and cellular organisms
Reaction Schemes
S-ubiquitinyl-[ubiquitin-carrier protein E2]-L-cysteine
+
[HECT-E3-ubiquitin-carrier protein]-L-cysteine
=
[ubiquitin-carrier protein E2]-L-cysteine
+
S-ubiquitinyl-[HECT-E3-ubiquitin-carrier protein]-L-cysteine
Synonyms
e3 ubiquitin-protein ligase, ubch5, e3 hect, ubcm3, e3 ubiquitin-protein ligase itchy homolog, more
SYNONYM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
E2-E3 ligase
-
E3 ubiquitin-protein ligase Itchy homolog
-
SYSTEMATIC NAME
IUBMB Comments
[ubiquitin-carrier protein E2]-S-ubiquitinyl-L-cysteine: [E3 acceptor protein] 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-[ubiquitin-carrier protein E2]-L-cysteine + [HECT-E3-ubiquitin-carrier protein]-L-cysteine
[ubiquitin-carrier protein E2]-L-cysteine + S-ubiquitinyl-[HECT-E3-ubiquitin-carrier protein]-L-cysteine
show the reaction diagram
-
-
-
?
additional information
?
-
the enzyme is autoinhibited by an intramolecular interaction between its HECT (homologous to the E6-AP carboxy terminus domain) and two central WW domains. Ndfip1 binds these WW domains to release the HECT, allowing trans-thiolation and enzyme catalytic activity
-
-
?
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-[ubiquitin-carrier protein E2]-L-cysteine + [HECT-E3-ubiquitin-carrier protein]-L-cysteine
[ubiquitin-carrier protein E2]-L-cysteine + S-ubiquitinyl-[HECT-E3-ubiquitin-carrier protein]-L-cysteine
show the reaction diagram
-
-
-
?
ORGANISM
COMMENTARY hide
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
isoform UbcM3
UniProt
Manually annotated by BRENDA team
GENERAL INFORMATION
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
physiological function
itch ligase activities are controlled via autoinhibition. Aberrant activation of Itch leads to migration defects of cortical neurons during development
UNIPROT
ENTRY NAME
ORGANISM
NO. OF AA
NO. OF TRANSM. HELICES
MOLECULAR WEIGHT[Da]
SOURCE
SEQUENCE
LOCALIZATION PREDICTION?
UB2E1_MOUSE
193
0
21333
Swiss-Prot
-
MOLECULAR WEIGHT
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
100000
x * 100000, SDS-PAGE
SUBUNIT
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
?
x * 100000, SDS-PAGE
PROTEIN VARIANTS
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
R600A
this HECT-domain mutant is inactive
Y763A
this HECT-domain mutant is inactive
additional information
generation of chimeric E2 enzymes consisting of different parts of human UbcH5 and murine UbcM3. Chimera consist of the N-terminal 62 amino acids of UbcH5 fused to the C-terminal 85 amino acids of UbcM3 and of the N-terminal 108 amino acids of UbcM3 fused to the C-terminal 85 amino acids of UbcH5, respectively. The ability to interact with E3 enzyme E6-AP maps to the C-terminal 85 amino acids of UbcH5
PURIFICATION (Commentary)
ORGANISM
UNIPROT
LITERATURE
Ni-NTA column chromatography or glutathione Sepharose column chromatography and gel filtration
CLONED (Commentary)
ORGANISM
UNIPROT
LITERATURE
expressed in Escherichia coli BL21(DE3) and HEK-293T cells
REF.
AUTHORS
TITLE
JOURNAL
VOL.
PAGES
YEAR
ORGANISM (UNIPROT)
PUBMED ID
SOURCE
Nuber, U.; Scheffner, M.
Identification of determinants in E2 ubiquitin-conjugating enzymes required for hect E3 ubiquitin-protein ligase interaction
J. Biol. Chem.
274
7576-7582
1999
Homo sapiens (P51668), Homo sapiens, Mus musculus (P52482)
Manually annotated by BRENDA team
Riling, C.; Kamadurai, H.; Kumar, S.; OLeary, C.E.; Wu, K.P.; Manion, E.E.; Ying, M.; Schulman, B.A.; Oliver, P.M.
Itch WW domains inhibit its E3 ubiquitin ligase activity by blocking E2-E3 ligase trans-thiolation
J. Biol. Chem.
290
23875-23887
2015
Mus musculus (Q8C863)
Manually annotated by BRENDA team
Zhu, K.; Shan, Z.; Chen, X.; Cai, Y.; Cui, L.; Yao, W.; Wang, Z.; Shi, P.; Tian, C.; Lou, J.; Xie, Y.; Wen, W.
Allosteric auto-inhibition and activation of the Nedd4 family E3 ligase Itch
EMBO Rep.
18
1618-1630
2017
Mus musculus (Q8C863), Homo sapiens (Q96J02)
Manually annotated by BRENDA team