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ATP + Oregon Green-labeled ubiquitin + [ubiquitin-activating protein E1]-L-cysteine
AMP + diphosphate + [ubiquitin-activating protein E1]-S-(Oregon Green-labeled ubiquitinyl)-L-cysteine
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enzyme efficiently accepts ubiquitin substrate fluorescently labeled by Oregon Green
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ATP + SUMO2 + [ubiquitin-activating protein UBA5]-L-cysteine
AMP + diphosphate + [ubiquitin-activating protein UBA5]-S-SUMO2-L-cysteine
SUMO2, small ubiquitin-like modifier2, an ubiquitin-like protein
enzyme greatly activates SUMO2 in the nucleus or transfers activated SUMO2 to the nucleus after it conjugated SUMO2 in the cytoplasm
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ATP + ubiquitin + SUMO2
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UBE1DC1 greatly activates SUMO2 in the nucleus or transfers activated-SUMO2 to nucleus after conjugation of SUMO2 in the cytoplasm
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ATP + ubiquitin + ubiquitin carrier protein E2
AMP + diphosphate + ubiquitin-(ubiquitin carrier protein E2)
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ATP + ubiquitin + ubiquitin-fold modifier 1
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ATP + ubiquitin + Ufm1
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ATP + ubiquitin + [6His-ubiquitin-activating enzyme E1]W-8His-Strep-HA
AMP + diphosphate + [6His-ubiquitin-activating enzyme E1]W-8His-Strep-HA-ubiquitinyl-L-cysteine
Strep, i.e.WSHPQFEK, HA, i.e. YPYDVPDYAS, under non-reducing conditions, the intermediate complex of the thioester formation is not observed without ATP
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ATP + ubiquitin + [E1 ubiquitin-activating enzyme]-L-cysteine
AMP + diphosphate + S-ubiquitinyl-[E1 ubiquitin-activating enzyme]-L-cysteine
ATP + ubiquitin + [ubiquitin-activating enzyme Uba5]-L-cysteine
AMP + diphosphate + [ubiquitin-activating enzyme Uba5]-S-ubiquitinyl-L-cysteine
the catalytic cysteine residue of isoform Uba5 is part of the adenylation domain in a alpha-helical motif
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ATP + ubiquitin + [ubiquitin-activating protein E1]-L-cysteine
AMP + diphosphate + [ubiquitin-activating protein E1]-S-ubiquitinyl-L-cysteine
ATP + ubiquitin + [ubiquitin-activating protein Uba1a]-L-cysteine
AMP + diphosphate + [ubiquitin-activating protein Uba1a]-S-ubiquitinyl-L-cysteine
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ATP + ubiquitin + [ubiquitin-activating protein UBA1]-L-cysteine
AMP + diphosphate + [ubiquitin-activating protein UBA1]-S-ubiquitinyl-L-cysteine
enzyme forms higher molecular mass intermediates with ubiquitin
the enzyme-ubiquitin intermediates dissociate in presence of 2-mercaptoethanol, indicating thiolester linkage
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ATP + ubiquitin + [ubiquitin-activating protein UBA2]-L-cysteine
AMP + diphosphate + [ubiquitin-activating protein UBA2]-S-ubiquitinyl-L-cysteine
enzyme forms higher molecular mass intermediates with ubiquitin
the enzyme-ubiquitin intermediates dissociate in presence of 2-mercaptoethanol, indicating thiolester linkage
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ATP + ubiquitin + [ubiquitin-activating protein Uba6]-L-cysteine
AMP + diphosphate + [ubiquitin-activating protein Uba6]-S-ubiquitinyl-L-cysteine
isoform Uba6 forms a covalent link with ubiquitin in vitro and in vivo, which is sensitive to reducing conditions. Recombinant E1 enzyme Uba6 can activate ubiquitin and transfer it onto the ubiquitin-conjugating enzyme UbcH5B. Ubiquitin activated by Uba6 can be used for ubiquitylation of p53 and supports the autoubiquitylation of the E3 ubiquitin ligases HectH9 and E6-AP
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ATP + ubiquitin + [ubiquitin-activating protein UBE1]-L-cysteine
AMP + diphosphate + [ubiquitin-activating protein UBE1]-S-ubiquitinyl-L-cysteine
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ATP + ubiquitin fold modifier1 + [ubiquitin-activating enzyme Uba5]-L-cysteine
AMP + diphosphate + [ubiquitin-activating enzyme Uba5]-S-(ubiquitin fold modifier1)-L-cysteine
the catalytic cysteine residue of isoform Uba5 is part of the adenylation domain in a alpha-helical motif
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ATP + ubiquitin mutant G76A + [ubiquitin-activating protein E1]-L-cysteine
AMP + diphosphate + [ubiquitin-activating protein E1]-S-(ubiquitin mutant G76A)yl-L-cysteine
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mutant ubiquitin G76A, bearing a Gly to Ala substitution at the COOH terminus is a substrate for El enzyme. Ubiquitin G76A supports PPI-ATP exchange with 500fold decrease in kcat/Km compared to wild-type ubiquitin, does not produce detectable AMP-Ub with native El, produces stoichiometric AMP-Ub with thiol-blocked El, gives a stoichiometric burst of ATP consumption with either native or thiol-blocked El, support El-ubiquitin thiol ester formation with native El, and supports several downstream reactions of the proteolytic pathway with a 20% decrease to the rate of wild type ubiquitin
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ATP + Ufm1 + [ubiquitin-activating protein UBA5]-L-cysteine
AMP + diphosphate + [ubiquitin-activating protein UBA5]-S-Ufm1-L-cysteine
Ufm1, ubiquitin-fold modifier 1, an ubiquitin-like protein
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additional information
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ATP + ubiquitin + [E1 ubiquitin-activating enzyme]-L-cysteine
AMP + diphosphate + S-ubiquitinyl-[E1 ubiquitin-activating enzyme]-L-cysteine
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ATP + ubiquitin + [E1 ubiquitin-activating enzyme]-L-cysteine
AMP + diphosphate + S-ubiquitinyl-[E1 ubiquitin-activating enzyme]-L-cysteine
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ATP + ubiquitin + [E1 ubiquitin-activating enzyme]-L-cysteine
AMP + diphosphate + S-ubiquitinyl-[E1 ubiquitin-activating enzyme]-L-cysteine
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ATP + ubiquitin + [E1 ubiquitin-activating enzyme]-L-cysteine
AMP + diphosphate + S-ubiquitinyl-[E1 ubiquitin-activating enzyme]-L-cysteine
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ATP + ubiquitin + [E1 ubiquitin-activating enzyme]-L-cysteine
AMP + diphosphate + S-ubiquitinyl-[E1 ubiquitin-activating enzyme]-L-cysteine
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ATP + ubiquitin + [E1 ubiquitin-activating enzyme]-L-cysteine
AMP + diphosphate + S-ubiquitinyl-[E1 ubiquitin-activating enzyme]-L-cysteine
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ATP + ubiquitin + [E1 ubiquitin-activating enzyme]-L-cysteine
AMP + diphosphate + S-ubiquitinyl-[E1 ubiquitin-activating enzyme]-L-cysteine
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ATP + ubiquitin + [E1 ubiquitin-activating enzyme]-L-cysteine
AMP + diphosphate + S-ubiquitinyl-[E1 ubiquitin-activating enzyme]-L-cysteine
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ATP + ubiquitin + [E1 ubiquitin-activating enzyme]-L-cysteine
AMP + diphosphate + S-ubiquitinyl-[E1 ubiquitin-activating enzyme]-L-cysteine
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ATP + ubiquitin + [E1 ubiquitin-activating enzyme]-L-cysteine
AMP + diphosphate + S-ubiquitinyl-[E1 ubiquitin-activating enzyme]-L-cysteine
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ATP + ubiquitin + [E1 ubiquitin-activating enzyme]-L-cysteine
AMP + diphosphate + S-ubiquitinyl-[E1 ubiquitin-activating enzyme]-L-cysteine
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ATP + ubiquitin + [E1 ubiquitin-activating enzyme]-L-cysteine
AMP + diphosphate + S-ubiquitinyl-[E1 ubiquitin-activating enzyme]-L-cysteine
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E1-activating enzyme activates ubiquitin via an adenylated intermediate and catalyzes its transfer to an E2 enzyme
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ATP + ubiquitin + [E1 ubiquitin-activating enzyme]-L-cysteine
AMP + diphosphate + S-ubiquitinyl-[E1 ubiquitin-activating enzyme]-L-cysteine
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E1 activates ubiquitin or an ubiquitin-like protein and transfers it to the E2-conjugating enzyme
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ATP + ubiquitin + [E1 ubiquitin-activating enzyme]-L-cysteine
AMP + diphosphate + S-ubiquitinyl-[E1 ubiquitin-activating enzyme]-L-cysteine
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ATP + ubiquitin + [E1 ubiquitin-activating enzyme]-L-cysteine
AMP + diphosphate + S-ubiquitinyl-[E1 ubiquitin-activating enzyme]-L-cysteine
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ATP + ubiquitin + [E1 ubiquitin-activating enzyme]-L-cysteine
AMP + diphosphate + S-ubiquitinyl-[E1 ubiquitin-activating enzyme]-L-cysteine
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ATP + ubiquitin + [E1 ubiquitin-activating enzyme]-L-cysteine
AMP + diphosphate + S-ubiquitinyl-[E1 ubiquitin-activating enzyme]-L-cysteine
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ATP + ubiquitin + [E1 ubiquitin-activating enzyme]-L-cysteine
AMP + diphosphate + S-ubiquitinyl-[E1 ubiquitin-activating enzyme]-L-cysteine
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ATP + ubiquitin + [ubiquitin-activating protein E1]-L-cysteine
AMP + diphosphate + [ubiquitin-activating protein E1]-S-ubiquitinyl-L-cysteine
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ATP + ubiquitin + [ubiquitin-activating protein E1]-L-cysteine
AMP + diphosphate + [ubiquitin-activating protein E1]-S-ubiquitinyl-L-cysteine
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a carboxylgroup is first activated as an adenylate followed by its direct transfer to an autonomous molecular moiety in a single enzymatic step
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ATP + ubiquitin + [ubiquitin-activating protein E1]-L-cysteine
AMP + diphosphate + [ubiquitin-activating protein E1]-S-ubiquitinyl-L-cysteine
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ATP + ubiquitin + [ubiquitin-activating protein E1]-L-cysteine
AMP + diphosphate + [ubiquitin-activating protein E1]-S-ubiquitinyl-L-cysteine
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additional information
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a lysine 48-linked polyubiquitin chain, assembled upon an internal lysine residue of a substrate protein, becomes the principle signal for recognition and target degradation by the 26S proteasome. E1 is not only essential for the initial ATP-dependent activation of ubiquitin in the ubiquitin degradtion pathway, but also capable of the catalytic extension of the polyubiquitin chain on a mono-ubiquitinated substrate
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additional information
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impaired nucleotide excision repair upon macrophage differentiation is corrected by E1 ubiquitin-activating enzyme
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additional information
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UBE1L2 transfers activated ubiquitin onto UbcH5b and supports E3-mediated polyubiquitylation
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additional information
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UBE1L2 transfers activated ubiquitin onto UbcH5b and supports E3-mediated polyubiquitylation
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additional information
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the thioester formation assay is performed using recombinant proteins expressed in Escherichia coli. The activation of ubiquitin by purified UBE1 is identified in vitro by SDS-PAGE
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additional information
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the thioester formation assay is performed using recombinant proteins expressed in Escherichia coli. The activation of ubiquitin by purified UBE1 is identified in vitro by SDS-PAGE
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additional information
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kinetics for Uba1a-catalyzed transthiolation of Ubc2b are used as a reporter assay for determining the Km and kcat values for the three cosubstrates of the ubiquitin-activating enzyme. The E2 transthiolation assays are more sensitive to the potential presence of trace catalytically active fragments than the single turnover end point assays used for quantitating ternary complex stoichiometry
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additional information
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purified isoform UBE1 can activate and conjugate ubiquitin to ubiquitin-conjugating enzyme E2s. Transfer is restricted to distinct E2 isoforms UB2R2, UBE2W and UBE2NL
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additional information
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purified isoform UBE1 can activate and conjugate ubiquitin to ubiquitin-conjugating enzyme E2s. Transfer is restricted to distinct E2 isoforms UB2R2, UBE2W and UBE2NL
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additional information
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residue Cys194 lies within a region of identity to active-site Cys88 of the ubiquitin carrier protein E2, suggesting a potential role for this region in enzymatic function. Residue Cys454 lies within a region of identity to the thiol ester consensus sequence of several proteins involved in thioester formation
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additional information
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residue Cys194 lies within a region of identity to active-site Cys88 of the ubiquitin carrier protein E2, suggesting a potential role for this region in enzymatic function. Residue Cys454 lies within a region of identity to the thiol ester consensus sequence of several proteins involved in thioester formation
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additional information
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E1 ubiquitin-activating enzyme UBA6 is the only E1 enzyme that can activate both ubiquitin and ubiquitin-like protein HLA-F adjacent transcript 10 (FAT10). FAT10 consists of two ubiquitin-like domains with 29% and 36% identity to ubiquitin, respectively, that are separated by a short linker region
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additional information
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orthogonal ubiquitin transfer (OUT) technology to profile their ubiquitination targets in mammalian cells of isozymes Uba1 and Uba6
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additional information
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orthogonal ubiquitin transfer (OUT) technology to profile their ubiquitination targets in mammalian cells of isozymes Uba1 and Uba6
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additional information
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CDC42 is a substrate of UBA6-initiated ubiquitination
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additional information
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CDC42 is a substrate of UBA6-initiated ubiquitination
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additional information
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the non-canonical E1, UBA5, binds to the ubiquitin-like protein UFM1 using a trans-binding mechanism in which UFM1 interacts with distinct sites in both subunits of the UBA5 dimer. Mechanism of UFM1 activation by UBA5 and trans-binding mechanism of UFM1 transfer to the E2, UFC1. UFM1 contains a C-terminal Val-Gly dipeptide instead of the canonical Gly-Gly dipeptide present in ubiquitin and other ubiquitin-like proteins
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additional information
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E1 consumes ATP and converts ubiquitin to a transfer-competent, enzyme-bound thioester. The reaction begins with ubiquitin-adenylate formation and the release of diphosohate. The active site cysteine of the E1 then displaces the AMP leading to a ubiquitin-E1 thioester complex
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additional information
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E1 consumes ATP and converts ubiquitin to a transfer-competent, enzyme-bound thioester. The reaction begins with ubiquitin-adenylate formation and the release of diphosohate. The active site cysteine of the E1 then displaces the AMP leading to a ubiquitin-E1 thioester complex
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additional information
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E1 activity is assesssed by the capacity of the enzyme to form a thiol ester conjugate with ubiquitin in an ATP-dependent process and to transfer this activated ubiquitin molecule to an conjugating enzyme
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additional information
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chimeric mutant Aos1-Uba2 SUMO-E1 enzyme shows SUMO-E1 activity. The E1 enzyme catalyzes the formation of a thioester-linked complex between SUMO and the E2 enzyme. This process is initiated by activation of the carboxyl terminus of SUMO by adenylation, followed by a thioesterification reaction in which SUMO is conjugated to a cysteine residue at the active site of Uba2 in the E1 enzyme. SUMO is then transferred to the active site cysteine of the E2 enzyme, Ubc9, via a trans-thioesterification reaction. A SUMO-charged E2 enzyme and substrate are finally bound with or without the assistance of a distinct class of SUMO E3-ligases, resulting in the activated SUMO bound to the substrate through an isopeptide linkage
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