Information on EC 2.3.2.B8 - E2:E3 ubiquitin transferase

Word Map on EC 2.3.2.B8
Please wait a moment until all data is loaded. This message will disappear when all data is loaded.
Specify your search results
Select one or more organisms in this record:
Show additional data
Do not include text mining results
Include (text mining) results (more...)
Include results (AMENDA + additional results, but less precise; more...)

The enzyme appears in viruses and cellular organisms

EC NUMBER
COMMENTARY hide
2.3.2.B8
preliminary BRENDA-supplied EC number
RECOMMENDED NAME
GeneOntology No.
E2:E3 ubiquitin transferase
-
REACTION
REACTION DIAGRAM
COMMENTARY hide
ORGANISM
UNIPROT
LITERATURE
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
SYSTEMATIC NAME
IUBMB Comments
[ubiquitin-carrier protein E2]-S-ubiquitinyl-L-cysteine: [E3 acceptor protein] ubiquitin transferase
-
ORGANISM
COMMENTARY hide
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
GENERAL INFORMATION
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
physiological function
part of the E1-E2-E3 ubiquitin conjugation cascade. The E2-ubiquitin covalent complex interacts with an E3 (HECT) for ubiquitin transfer. Ubiquitin is transferred to the acceptor cysteine of the C-lobe of the HECT domain; part of the E1-E2-E3 ubiquitin conjugation cascade. The E2-ubiquitin covalent complex interacts with an E3 (HECT) for ubiquitin transfer. Ubiquitin is transferred to the acceptor cysteine of the C-lobe of the HECT domain
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 cIAP2]-L-cysteine
[ubiquitin-carrier protein E2]-L-cysteine + S-ubiquitinyl-[HECT-E3-ubiquitin-carrier protein cIAP2]-L-cysteine
show the reaction diagram
-
-
-
-
?
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
[ubiquitin-carrier protein UbcH5]-S-ubiquitinyl-L-cysteine + [HECT-E3-ubiquitin-carrier protein E6-AP]-L-cysteine
[ubiquitin-carrier protein UbcH5]-L-cysteine + [HECT-E3-ubiquitin-carrier protein E6-AP]-S-ubiquitinyl-L-cysteine
show the reaction diagram
a region of isoform UbcH5 encompassing the catalytic site cysteine residue is critical for its ability to interact with E3 enzymes E6-AP and RSP5. Of particular importance is a phenylalanine residue at position 62 of UbcH5 that is conserved among the members of the UBC4/UBC5 subfamily but is not present in any of the other known E2s
-
-
-
[ubiquitin-carrier protein UbcH5]-S-ubiquitinyl-L-cysteine + [HECT-E3-ubiquitin-carrier protein Rsp5]-L-cysteine
[ubiquitin-carrier protein UbcH5]-L-cysteine + [HECT-E3-ubiquitin-carrier protein Rsp5]-S-ubiquitinyl-L-cysteine
show the reaction diagram
a region of isoform UbcH5 encompassing the catalytic site cysteine residue is critical for its ability to interact with E3 enzymes E6-AP and RSP5. Of particular importance is a phenylalanine residue at position 62 of UbcH5 that is conserved among the members of the UBC4/UBC5 subfamily but is not present in any of the other known E2s
-
-
-
additional information
?
-
NATURAL SUBSTRATES
NATURAL PRODUCTS
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
MOLECULAR WEIGHT
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
21400
-
1 * 21400, calculated from amino acid sequence
22400
-
1 * 22400, SEC-MALS analysis
100000
x * 100000, SDS-PAGE
SUBUNITS
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
?
x * 100000, SDS-PAGE
monomer
-
1 * 21400, calculated from amino acid sequence; 1 * 22400, SEC-MALS analysis
Crystallization/COMMENTARY
ORGANISM
UNIPROT
LITERATURE
determination of the crystal of a complex between the HECT domain NEDD4L and the E2 UbcH5B bearing a covantly-linked ubiquitin at its active site to gain insights of the ubiquitin transfer from an associated E2 to the acceptor cysteine in the HECT domain C-lobe. HECT contains is bilobed, consists of N-terminal N-lobe and C-terminal C-lobe. The C-lobe is essential for the E2-to-E3 ubiquitin transfer and the N-lobe is essential for the the further protein substrate processivity, the transfer of the ubiquitin from E3 to the substrate; determination of the crystal of a complex between the HECT domain NEDD4L and the E2 UbcH5B bearing a covantly-linked ubiquitin at its active site to gain insights of the ubiquitin transfer from an associated E2 to the acceptor cysteine in the HECT domain C-lobe. HECT contains is bilobed, consists of N-terminal N-lobe and C-terminal C-lobe. The C-lobe is essential for the E2-to-E3 ubiquitin transfer and the N-lobe is essential for the the further protein substrate processivity, the transfer of the ubiquitin from E3 to the substrate
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
ENGINEERING
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
S68A
-
the mutant shows wild type activity
R600A
this HECT-domain mutant is inactive
Y763A
this HECT-domain mutant is inactive
additional information