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Information on EC 2.3.2.27 - RING-type E3 ubiquitin transferase and Organism(s) Saccharomyces cerevisiae and UniProt Accession P40318

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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.
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Saccharomyces cerevisiae
UNIPROT: P40318
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Word Map
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The taxonomic range for the selected organisms is: Saccharomyces cerevisiae
The enzyme appears in selected viruses and cellular organisms
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
[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
ERAD-associated E3 ubiquitin-protein ligase DOA10
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ERAD-associated E3 ubiquitin-protein ligase HRD1
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pre-mRNA-splicing factor 19
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RING-finger ubiquitin ligase Ubr1
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ubiquitin ligase E3
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ubiquitin ligase Ubr1
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REACTION
REACTION DIAGRAM
COMMENTARY hide
ORGANISM
UNIPROT
LITERATURE
[E2 ubiquitin-conjugating enzyme]-S-ubiquitinyl-L-cysteine + [acceptor protein]-L-lysine = [E2 ubiquitin-conjugating enzyme]-L-cysteine + [acceptor protein]-N6-ubiquitinyl-L-lysine
show the reaction diagram
Ubr1 is an ubiquitin ligase, which is able to recignize N-end rule substrates. These substrates occur at two sites, type1 and type-2, specific for reecognition of basic N-terminal amino acid residues and responsible for recognition of bulky hydrophobic amino acid residues of proteins
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PATHWAY SOURCE
PATHWAYS
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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.
SUBSTRATE
PRODUCT                       
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate) hide
LITERATURE
(Substrate)
COMMENTARY
(Product) hide
LITERATURE
(Product)
Reversibility
r=reversible
ir=irreversible
?=not specified
additional information
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degradation of the cytoplasmic misfolded protein DELTAssCL*myc, a derivative of signal sequence delted mutated carboxypeptidase yscY
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?
ORGANISM
COMMENTARY hide
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
LOCALIZATION
ORGANISM
UNIPROT
COMMENTARY hide
GeneOntology No.
LITERATURE
SOURCE
GENERAL INFORMATION
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
physiological function
in vivo degradation of substrates for integral endoplasmic reticulum membrane E3 ubiquitin ligase Doa10 is inhibitied by mutations in the alpha2 helix of E2 enzyme Ubc7 by preventing the conjugation of donor ubiquitin to the acceptor. Ubiquitin chain formation by mutant Ubc7 is not restored by the E3 enzyme Doa10 RING domain. alpha2 Helix mutations selectively impair the in vivo degradation of Doa10 substrates
physiological function
CRYSTALLIZATION (Commentary)
ORGANISM
UNIPROT
LITERATURE
structure of fragment Prp19(1-133), which contains both the N-terminal U-box and central coiled-coil domain, to 1.38 A resolution. The Prp19 U-box domain exists in a dimeric state in the context of intact Prp19. The hydrophobic character of the dimer interface is due to residues Leu15, Ile22, Val51, and Ile53. All four positions are conserved long-chain hydrophobic residues
PROTEIN VARIANTS
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
K118R
residue Lys118 is required for Ubc7 activity. Mutant is very poor in assembly of polyubiquitin chains. Lys118 is both essential and sufficient for Doa10-mediated degradation of substrates
K118R
residue Lys118 is required for Ubc7 activity. Mutant is very poor in assembly of polyubiquitin chains. Lys118 is both essential and sufficient for Doa10-mediated degradation of substrates
L15E
mutant in U-box domain interface, abrogates U-box dimer formation and is lethal in vivo
REF.
AUTHORS
TITLE
JOURNAL
VOL.
PAGES
YEAR
ORGANISM (UNIPROT)
PUBMED ID
SOURCE
Vander Kooi, C.W.; Ohi, M.D.; Rosenberg, J.A.; Oldham, M.L.; Newcomer, M.E.; Gould, K.L.; Chazin, W.J.
The Prp19 U-box crystal structure suggests a common dimeric architecture for a class of oligomeric E3 ubiquitin ligases
Biochemistry
45
121-130
2006
Saccharomyces cerevisiae (P32523)
Manually annotated by BRENDA team
Eisele, F.; Wolf, D.H.
Degradation of misfolded protein in the cytoplasm is mediated by the ubiquitin ligase Ubr1
FEBS Lett.
582
4143-4146
2008
Saccharomyces cerevisiae
Manually annotated by BRENDA team
Cohen, I.; Wiener, R.; Reiss, Y.; Ravid, T.
Distinct activation of an E2 ubiquitin-conjugating enzyme by its cognate E3 ligases
Proc. Natl. Acad. Sci. USA
112
E625-E632
2015
Saccharomyces cerevisiae (P40318), Saccharomyces cerevisiae (Q08109)
Manually annotated by BRENDA team