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Information on EC 2.3.2.B8 - E2:E3 ubiquitin transferase and Organism(s) Homo sapiens
for references in articles please use BRENDA:EC2.3.2.B8preliminary BRENDA-supplied EC number
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2.3.2.B8 E2:E3 ubiquitin transferaseSpecify your search results
The taxonomic range for the selected organisms is: Homo sapiens
The enzyme appears in selected viruses and cellular organisms
The enzyme appears in selected viruses and cellular organisms
Reaction Schemes
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S-ubiquitinyl-[ubiquitin-carrier protein E2]-L-cysteine
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[HECT-E3-ubiquitin-carrier protein]-L-cysteine
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[ubiquitin-carrier protein E2]-L-cysteine
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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
topSYNONYM 
ORGANISM
UNIPROT
COMMENTARY 
LITERATURE
REACTION
REACTION DIAGRAM
COMMENTARY
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
the 40 kDa C-terminal HET domain binds a reactive thioester-linked E2-ubiquitin covalent-linked complex. The ubiqiutin is transferred from the E2 catalytic cysteine to the HECT domain catalytic cysteine via a transthiolation reaction
SYSTEMATIC NAME
IUBMB Comments
[ubiquitin-carrier protein E2]-S-ubiquitinyl-L-cysteine: [E3 acceptor protein] ubiquitin transferase
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SUBSTRATE
PRODUCT
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate)
(Substrate)
LITERATURE
(Substrate)
(Substrate)
COMMENTARY
(Product)
(Product)
LITERATURE
(Product)
(Product)
Reversibility
r=reversible
ir=irreversible
?=not specified
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
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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
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[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
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
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[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
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
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additional information
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the full-length UBE2E proteins primarily promote protein monoubiquitylation, whereas the core UBC domain of each can efficiently build polyubiquitin chains
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additional information
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the N-terminal extension of Ube2E1 undergoes intramolecular auto-ubiquitination. This self-ubiquitination activity is enhanced in the presence of interacting RING E3 ligases like RNF4 and results in a progressive attenuation of the E2 activity toward substrate/E3 modification
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NATURAL SUBSTRATE
NATURAL PRODUCT
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate)
(Substrate)
LITERATURE
(Substrate)
(Substrate)
COMMENTARY
(Product)
(Product)
LITERATURE
(Product)
(Product)
REVERSIBILITY
r=reversible
ir=irreversible
?=not specified
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
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-
-
-
?
ORGANISM
COMMENTARY
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
GENERAL INFORMATION
ORGANISM
UNIPROT
COMMENTARY
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
UNIPROT
ENTRY NAME
ORGANISM
NO. OF AA
NO. OF TRANSM. HELICES
MOLECULAR WEIGHT[Da]
SOURCE
SEQUENCE
LOCALIZATION PREDICTION
The reliability class of the localization prediction ranges from 1 (very reliable) to 5 (not reliable).
The reliability class of the localization prediction ranges from 1 (very reliable) to 5 (not reliable). MOLECULAR WEIGHT
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
SUBUNIT
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
monomer
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
the WW domains proceeding the catalytic HECT domain play an inhibitory role by binding directly to HECT. The WW2 domain and a following linker allosterically lock HECT in an inactive state inhibiting E2-E3 transthiolation. Binding of the Ndfip1 adaptor or JNK1-mediated phosphorylation relieves the auto-inhibition of Itch in a WW2-dependent manner
PROTEIN VARIANTS
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
additional information
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 and particularly to 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 E2 enzymes
additional information
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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 and particularly to 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 E2 enzymes
CLONED (Commentary)
ORGANISM
UNIPROT
LITERATURE
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)
Kamadurai, H.B.; Souphron, J.; Scott, D.C.; Duda, D.M.; Miller, D.J.; Stringer, D.; Piper, R.C.; Schulman, B.A.
Insights into ubiquitin transfer cascades from a structure of a UbcH5B approximately ubiquitin-HECT(NEDD4L) complex
Mol. Cell.
36
1095-1102
2009
Homo sapiens (P62837), Homo sapiens (Q96PU5)
Schumacher, F.R.; Wilson, G.; Day, C.L.
The N-terminal extension of UBE2E ubiquitin-conjugating enzymes limits chain assembly
J. Mol. Biol.
425
4099-4111
2013
Homo sapiens
Banka, P.A.; Behera, A.P.; Sarkar, S.; Datta, A.B.
RING E3-catalyzed E2 self-ubiquitination attenuates the activity of Ube2E ubiquitin-conjugating enzymes
J. Mol. Biol.
427
2290-2304
2015
Homo sapiens
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