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Information on EC 2.3.2.8 - arginyltransferase
for references in articles please use BRENDA:EC2.3.2.8Please wait a moment until all data is loaded. This message will disappear when all data is loaded.
EC Tree
2.3.2.8 arginyltransferaseIUBMB Comments
Requires 2-sulfanylethan-1-ol (2-mercaptoethanol) and a univalent cation. Peptides and proteins containing an N-terminal glutamate, aspartate or cystine residue can act as acceptors.
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Word Map
- 2.3.2.8
-
arginylation
-
2.5.1.18
-
rx:glutathione
- rx
-
n-degrons
-
polyubiquitylates
- medicine
- agriculture
The expected taxonomic range for this enzyme is: Eukaryota, Bacteria, Archaea
Synonyms
arginyltransferase, r-transferase, arginyl-trna-protein transferase, arginyl-trna protein transferase, arginyltransferase 1, arginyl transferase, arg-transferase, arginyl-trna:protein arginyltransferase, arginyl-transferase, ate1-1, 
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SYNONYM 
ORGANISM
UNIPROT
COMMENTARY 
LITERATURE
Arg-transferase
Arg-tRNA-protein transferase
arginyl tRNA transferase
-
-
-
-
arginyl-transfer ribonucleate-protein aminoacyltransferase
-
-
-
-
arginyl-transfer ribonucleate-protein transferase
-
-
-
-
arginyl-transferase
arginyl-tRNA protein transferase
arginyl-tRNA--protein transferase
arginyl-tRNA-protein transferase
arginyltransferase
arginyltransferase 1
ATE
Ate1
Ate1-3
Ate1-4
DdAte1
L-arginyltransferase
-
-
-
-
R-transferase
arginyl-tRNA protein transferase
-
-
-
-
R-transferase
-
-
-
-
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REACTION
REACTION DIAGRAM
COMMENTARY
ORGANISM
UNIPROT
LITERATURE
L-arginyl-tRNAArg + protein = tRNAArg + L-arginyl-[protein]
-
-
-
-
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REACTION TYPE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
Acyl group transfer
arginylation
Acyl group transfer
-
-
-
-
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PATHWAY SOURCE
PATHWAYS
-
-
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SYSTEMATIC NAME
IUBMB Comments
L-arginyl-tRNAArg:protein arginyltransferase
Requires 2-sulfanylethan-1-ol (2-mercaptoethanol) and a univalent cation. Peptides and proteins containing an N-terminal glutamate, aspartate or cystine residue can act as acceptors.
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CAS REGISTRY NUMBER
COMMENTARY
37257-24-2
-
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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
L-Arg-tRNA + apolipoprotein A-I
tRNAArg + L-Arg-[apolipoprotein A-I]
-
-
-
-
?
L-Arg-tRNAArg + alpha-1-antitrypsin
tRNAArg + L-Arg-[alpha-1-antitrypsin]
-
-
-
-
?
L-Arg-tRNAArg + apolipoprotein E
tRNAArg + L-Arg-[apolipoprotein E]
-
-
-
-
?
L-Arg-tRNAArg + contrapsin-like protease inhibitor-3
tRNAArg + L-Arg-[contrapsin-like protease inhibitor-3]
-
-
-
-
?
L-Arg-tRNAArg + Cys-beta-galactosidase
tRNaArg + L-Arg-L-Cys-beta-galactosidase
-
substrate only for isoforms Ate1-3, Ate1-4
-
-
?
L-Arg-tRNAArg + glucose-related protein 78
tRNAArg + L-Arg-[glucose-related protein 78]
-
-
-
-
?
L-Arg-tRNAArg + protein-disulfide isomerase
tRNAArg + L-Arg-[protein-disulfide isomerase]
-
-
-
-
?
L-arginyl-tRNA + L-Asp-beta-galactosidase
tRNA + L-arginyl-L-Asp-beta-galactosidase
-
-
-
-
?
L-arginyl-tRNAArg + alpha cardiac actin
tRNAArg + L-arginyl-[alpha cardiac actin]
-
-
-
?
L-arginyl-tRNAArg + alpha-synuclein
tRNAArg + L-arginyl-[alpha-synuclein]
alpha-syn is arginylated in vitro and in vivo
-
-
?
L-arginyl-tRNAArg + Asp-beta-galactosidase
tRNAArg + L-arginyl-Asp-beta-galactosidase
-
-
-
-
?
L-arginyl-tRNAArg + BiP/GRP78 protein
tRNAArg + L-arginyl-[BiP/GRP78 protein]
-
-
-
-
?
L-arginyl-tRNAArg + bovine alpha-lactalbumin
tRNAArg + L-arginyl-[bovine alpha-lactalbumin]
-
higher activity is detected with isoforms ATE1-1 (100%) and ATE1-2 (85%), and weaker activity is detected with isoforms ATE1-3 (18%) and ATE1-4 (4%)
-
-
?
L-arginyl-tRNAArg + calreticulin
tRNAArg + L-arginyl-[calreticulin]
-
-
-
-
?
L-arginyl-tRNAArg + EBP
tRNAArg + L-arginyl-[EBP]
Pseudomonas syringae ethylene response factor 72 (EBP) is a putative substrate for ATE1
-
-
?
L-arginyl-tRNAArg + fructose diphosphatase
tRNAArg + L-Arg-[fructose diphosphatase]
-
from rabbit liver
-
-
?
L-arginyl-tRNAArg + immunoglobulin
tRNAArg + L-arginyl-[immunoglobulin]
-
kappa-light chain of immunoglobulin
-
-
?
L-arginyl-tRNAArg + L-Arg-[beta-galactosidase]
tRNAArg + L-Arg-L-Arg-[beta-galactosidase]
-
-
-
-
?
L-arginyl-tRNAArg + L-Asp-L-Ala
tRNAArg + L-Arg-L-Asp-L-Ala
-
other dipeptides: overview
-
-
?
L-arginyl-tRNAArg + L-aspartic acid
tRNAArg + L-Arg-L-Asp
-
poor substrate
-
?
L-arginyl-tRNAArg + L-cystinyl-bis-L-Ala
tRNAArg + L-Arg-L-cystinyl-bis-L-Ala
-
poor substrate
-
-
?
L-arginyl-tRNAArg + L-Glu-L-Ala
tRNAArg + L-Arg-L-Glu-L-Ala
-
other dipeptides: overview, not dipeptides with D-Glu
-
?
L-arginyl-tRNAArg + L-Glu-L-Ala-L-Ala
tRNAArg + L-Arg-L-Glu-L-Ala-L-Ala
-
other tripeptides: overview
-
-
?
L-arginyl-tRNAArg + L-Glu-[beta-galactosidase]
tRNAArg + L-Arg-L-Glu-[beta-galactosidase]
-
-
-
-
?
L-arginyl-tRNAArg + L-glutamic acid
tRNAArg + L-Arg-L-Glu
-
poor substrate
-
?
L-arginyl-tRNAArg + L-isoasparagine
tRNAArg + L-arginyl-L-isoasparagine
-
non-peptide-derivatives of dicarboxylic amino acids with blocked alpha-carboxyl group and unsubstituted beta- or gamma-carboxyl group, such as isoasparagine and isoglutamine
-
-
?
L-arginyl-tRNAArg + L-isoglutamine
tRNAArg + L-arginyl-L-isoglutamine
-
non-peptide-derivatives of dicarboxylic amino acids with blocked alpha-carboxyl group and unsubstituted beta- or gamma-carboxyl group, such as isoasparagine and isoglutamine
-
-
?
L-arginyl-tRNAArg + L-Met-[beta-galactosidase]
tRNAArg + L-Arg-L-Met-[beta-galactosidase]
-
-
-
-
?
L-arginyl-tRNAArg + N-L-aspartyl-N'-dansylamido-1,4-butanediamine
tRNAArg + N-(L-arginyl-L-aspartyl)-N'-dansylamido-1,4-butanediamine
L-arginyl-tRNAArg + protein disulfide isomerase
tRNAArg + L-arginyl-[protein disulfide isomerase]
-
-
-
-
?
L-arginyl-tRNAArg + Rgs16 regulator of G protein
tRNAArg + L-arginyl-[Rgs16 regulator of G protein]
-
-
-
?
L-arginyl-tRNAArg + Rgs4 regulator of G protein
tRNAArg + L-arginyl-[Rgs4 regulator of G protein]
-
-
-
?
L-arginyl-tRNAArg + Rgs5 regulator of G protein
tRNAArg + L-arginyl-[Rgs5 regulator of G protein]
-
-
-
?
L-arginyl-tRNAArg + RIN4
tRNAArg + L-arginyl-[RIN4]
Pseudomonas syringae 1-interacting protein 4 (RIN4) is a putative substrate for ATE1
-
-
?
L-arginyl-tRNAArg + transaldolase
tRNAArg + L-arginyl-[transaldolase]
-
I and III from Candida
-
-
?
L-arginyl-tRNAArg + trypsin inhibitor
tRNAArg + L-arginyl-[trypsin inhibitor]
-
from soybean
-
-
?
L-arginyl-tRNAArg + VRN2
tRNAArg + L-arginyl-[VRN2]
Pseudomonas syringae vernalization 2 protein (VRN2) is a putative substrate for ATE1
-
-
?
L-arginyl-tRNAArg + acceptor protein
tRNAArg + L-arginyl-[acceptor protein]
-
-
-
?
L-arginyl-tRNAArg + acceptor protein
tRNAArg + L-arginyl-[acceptor protein]
-
-
-
-
?
L-arginyl-tRNAArg + acceptor protein
tRNAArg + L-arginyl-[acceptor protein]
-
-
-
?
L-arginyl-tRNAArg + acceptor protein
tRNAArg + L-arginyl-[acceptor protein]
ATE1-2p is less active than ATE1-1p
-
-
?
L-arginyl-tRNAArg + acceptor protein
tRNAArg + L-arginyl-[acceptor protein]
-
addition to amino-terminus
-
-
?
L-arginyl-tRNAArg + acceptor protein
tRNAArg + L-arginyl-[acceptor protein]
-
involved in ubiquitin mediated protein degradation
-
-
?
L-arginyl-tRNAArg + acceptor protein
tRNAArg + L-arginyl-[acceptor protein]
-
-
-
-
?
L-arginyl-tRNAArg + acceptor protein
tRNAArg + L-arginyl-[acceptor protein]
-
addition to amino-terminus
-
-
?
L-arginyl-tRNAArg + acceptor protein
tRNAArg + L-arginyl-[acceptor protein]
-
-
-
-
?
L-arginyl-tRNAArg + acceptor protein
tRNAArg + L-arginyl-[acceptor protein]
-
-
-
?
L-arginyl-tRNAArg + acceptor protein
tRNAArg + L-arginyl-[acceptor protein]
-
-
-
?
L-arginyl-tRNAArg + acceptor protein
tRNAArg + L-arginyl-[acceptor protein]
-
-
-
?
L-arginyl-tRNAArg + acceptor protein
tRNAArg + L-arginyl-[acceptor protein]
-
acceptor proteins require an acidic amino terminus, an Asp- or Glu-residue at the acceptor site
-
?
L-arginyl-tRNAArg + acceptor protein
tRNAArg + L-arginyl-[acceptor protein]
-
addition to amino-terminus
-
?
L-arginyl-tRNAArg + acceptor protein
tRNAArg + L-arginyl-[acceptor protein]
-
possibly involved in degradation of proteins with acidic NH2-termini
-
-
?
L-arginyl-tRNAArg + acceptor protein
tRNAArg + L-arginyl-[acceptor protein]
-
catalyzes post-translational ribosome-independent modification of certain acceptor proteins
-
-
?
L-arginyl-tRNAArg + acceptor protein
tRNAArg + L-arginyl-[acceptor protein]
-
-
-
?
L-arginyl-tRNAArg + acceptor protein
tRNAArg + L-arginyl-[acceptor protein]
-
-
-
-
?
L-arginyl-tRNAArg + acceptor protein
tRNAArg + L-arginyl-[acceptor protein]
-
-
-
?
L-arginyl-tRNAArg + acceptor protein
tRNAArg + L-arginyl-[acceptor protein]
-
-
-
?
L-arginyl-tRNAArg + acceptor protein
tRNAArg + L-arginyl-[acceptor protein]
-
involved in ubiquitin mediated protein degradation
-
-
?
L-arginyl-tRNAArg + acceptor protein
tRNAArg + L-arginyl-[acceptor protein]
-
-
-
?
L-arginyl-tRNAArg + acceptor protein
tRNAArg + L-arginyl-[acceptor protein]
-
-
-
?
L-arginyl-tRNAArg + albumin
tRNAArg + L-arginyl-albumin
-
from bovine serum
-
-
?
L-arginyl-tRNAArg + albumin
tRNAArg + L-arginyl-albumin
-
from bovine serum, accepts 1 mol arginine/mol
-
-
?
L-arginyl-tRNAArg + alpha lactalbumin
tRNAArg + L-arginyl-[lactalbumin]
-
-
-
-
?
L-arginyl-tRNAArg + alpha lactalbumin
tRNAArg + L-arginyl-[lactalbumin]
-
bovine
-
-
?
L-arginyl-tRNAArg + beta-actin
tRNAArg + L-arginyl-[beta-actin]
-
-
-
?
L-arginyl-tRNAArg + beta-actin
tRNAArg + L-arginyl-[beta-actin]
-
-
-
?
L-arginyl-tRNAArg + bovine serum albumin
tRNAArg + L-arginyl-[bovine serum albumin]
-
-
-
-
?
L-arginyl-tRNAArg + bovine serum albumin
tRNAArg + L-arginyl-[bovine serum albumin]
-
high activity is detected with isoforms ATE1-1 (100%) and ATE1-2 (95%), and weaker activity is detected with isoforms ATE1-3 (10%) and ATE1-4 (4%)
-
-
?
L-arginyl-tRNAArg + ERF-VII peptide
tRNAArg + L-arginyl-[ERF-VII peptide]
after N-terminal Cys-sulfinic acid formation on ERF-VII peptide through plant cysteine oxidase. An ERF-VII peptide with an N-terminal Gly does not accept Arg, whereas an N-terminal Asp accepts Arg, independent of the presence of PCO1 or 4. A peptide comprising an N-terminal Cys-sulfonic acid is also shown to be a substrate for ATE1, again independent of the presence of PCO1 or 4. Proposed arginylation requirements for the Arg/Cys branch of the N-end rule pathway
-
-
?
L-arginyl-tRNAArg + ERF-VII peptide
tRNAArg + L-arginyl-[ERF-VII peptide]
after N-terminal Cys-sulfinic acid formation on ERF-VII peeptide through plant cysteine oxidase. C-terminally biotinylated RAP22-13 peptides (H2N-XGGAIISDFIPP(PEG)K(biotin)-NH2) where the N-terminal residue, X, constitutes Gly, Asp, Cys or Cys-sulfonic acid are subjected to the arginylation assay in the presence or absence of PCO1/4. An ERF-VII peptide with an N-terminal Gly does not accept Arg, whereas an N-terminal Asp accepts Arg, independent of the presence of PCO1 or 4. A peptide comprising an N-terminal Cys-sulfonic acid is also shown to be a substrate for ATE1, again independent of the presence of PCO1 or 4. Arginylation of the 12-mer peptide substrates, peptide sequences, overview
-
-
?
L-arginyl-tRNAArg + insulin
tRNAArg + L-arginyl-[insulin]
-
less effective
-
-
?
L-arginyl-tRNAArg + N-L-aspartyl-N'-dansylamido-1,4-butanediamine
tRNAArg + N-(L-arginyl-L-aspartyl)-N'-dansylamido-1,4-butanediamine
-
-
-
-
?
L-arginyl-tRNAArg + N-L-aspartyl-N'-dansylamido-1,4-butanediamine
tRNAArg + N-(L-arginyl-L-aspartyl)-N'-dansylamido-1,4-butanediamine
-
i.e. Asp(4)DNS
i.e. ArgAsp(4)DNS
?
L-arginyl-tRNAArg + protein
tRNAArg + L-arginyl-[protein]
-
-
-
?
L-arginyl-tRNAArg + protein
tRNAArg + L-arginyl-[protein]
-
-
-
?
L-arginyl-tRNAArg + protein
tRNAArg + L-arginyl-[protein]
-
-
-
?
L-arginyl-tRNAArg + protein
tRNAArg + L-arginyl-[protein]
-
-
-
?
L-arginyl-tRNAArg + protein
tRNAArg + L-arginyl-[protein]
-
-
-
-
?
L-arginyl-tRNAArg + protein
tRNAArg + L-arginyl-[protein]
-
-
-
?
L-arginyl-tRNAArg + protein
tRNAArg + L-arginyl-[protein]
-
the enzyme catalyzes mid-chain arginylation of proteins at side chain carboxylates in vivo. N-terminal arginylation of the peptide substrates occurs by the alpha amino group
-
-
?
L-arginyl-tRNAArg + protein
tRNAArg + L-arginyl-[protein]
-
-
-
?
L-arginyl-tRNAArg + protein
tRNAArg + L-arginyl-[protein]
-
-
-
?
L-arginyl-tRNAArg + protein
tRNAArg + L-arginyl-[protein]
-
-
-
?
L-arginyl-tRNAArg + protein
tRNAArg + L-arginyl-[protein]
-
-
-
-
?
L-arginyl-tRNAArg + protein
tRNAArg + L-arginyl-[protein]
-
-
-
-
?
L-arginyl-tRNAArg + RGS4 protein
tRNAArg + L-arginyl-[RGS4 protein]
-
-
-
?
L-arginyl-tRNAArg + RGS4 protein
tRNAArg + L-arginyl-[RGS4 protein]
Mus musculus 129SvEv/C57BL/6
-
-
-
?
L-arginyl-tRNAArg + thyroglobulin
tRNAArg + L-arginyl-[thyroglobulin]
-
-
-
-
?
L-arginyl-tRNAArg + thyroglobulin
tRNAArg + L-arginyl-[thyroglobulin]
-
accepts 2 mol arginine/mol
-
-
?
additional information
?
-
putative substrates of ATE are identified among Nt Met-Cys proteins. N-terminal Asp, Glu, or oxidized Cys on peptides and proteins are ATE substrates
-
-
-
additional information
?
-
N-terminal Asp, Glu, or oxidized Cys on peptides and proteins are ATE substrates
-
-
-
additional information
?
-
identification of four arginylation sites in the most abundant actin isoform of Dictyostelium discoideum, in addition to arginylation sites in other actin isoforms and several actin-binding proteins
-
-
-
additional information
?
-
-
identification of four arginylation sites in the most abundant actin isoform of Dictyostelium discoideum, in addition to arginylation sites in other actin isoforms and several actin-binding proteins
-
-
-
additional information
?
-
identification of four arginylation sites in the most abundant actin isoform of Dictyostelium discoideum, in addition to arginylation sites in other actin isoforms and several actin-binding proteins
-
-
-
additional information
?
-
the Arg/N-end rule-mediated autophagic flux regulator might be a direct substrate of ATE1, rather than UBR1 or UBR2
-
-
-
additional information
?
-
usage of DD-bta15-GFP assay for an 'in-lysate' reaction to examine arginylation activity in cell extracts
-
-
-
additional information
?
-
-
usage of DD-bta15-GFP assay for an 'in-lysate' reaction to examine arginylation activity in cell extracts
-
-
-
additional information
?
-
-
isoforms Ate1-3, Ate1-4, no substrate: proteins containing N-terminal Asp or Glu
-
-
?
additional information
?
-
-
ATE1 is capable of self-arginylation in vitro and in vivo
-
-
?
additional information
?
-
-
the arginylation reaction does not require the formation of an ATE1-arginyl-tRNA synthetase complex or the presence of ATP
-
-
?
additional information
?
-
-
Liat1 protein binds to the mouse Ate1 enzyme, but is apparently not arginylated by it
-
-
?
additional information
?
-
the Arg/N-end rule-mediated autophagic flux regulator might be a direct substrate of ATE1, rather than UBR1 or UBR2
-
-
-
additional information
?
-
the four mouse ATE1 isoforms have different, partially overlapping substrate specificity toward their N-terminal target sites, detailed overview. The four mouse ATE1 isoforms show prominent and consistent differences in target site specificity, both at the N-terminus and the side chain sites. At the N-terminal sites, only three of the four ATE1 isoforms (ATE1-1, 2, and 3) show high preference for the peptides containing N-terminal D and E. ATE1-4 do not appear to target peptides containing N-terminal E. At the same time all four isoforms, to a various degree, show prominent reactivity with the peptides bearing N-terminal C. Even more strikingly, ATE1-1, unlike any other ATE1 isoforms, appears to be reactive with additional N-terminal sites not seen with other ATE1 isoforms, including Q and, weakly, H. Thus, it appears that N-terminal target site specificity of ATE1-1 may be broader than other ATE1 isoforms and potentially include non-canonical N-terminal residues. The four ATE1 isoforms also show different reactivity with the peptides bearing side chain target sites. In the case of ATE1-1 and ATE1-2, the signal with these peptides containing side chain target sites is substantially lower or absent compared to the peptides containing favorable N-terminal target sites. Side chain arginylation of one of these peptides with ATE1-2 in solution. It appears likely that the peptide array format is unfavorable for side chain targeting by these ATE1 isoforms. Isozyme ATE1-1 catalyzes arginylation of non-canonical residues. Identification of the arginylation-favorable sequence motif
-
-
-
additional information
?
-
-
the four mouse ATE1 isoforms have different, partially overlapping substrate specificity toward their N-terminal target sites, detailed overview. The four mouse ATE1 isoforms show prominent and consistent differences in target site specificity, both at the N-terminus and the side chain sites. At the N-terminal sites, only three of the four ATE1 isoforms (ATE1-1, 2, and 3) show high preference for the peptides containing N-terminal D and E. ATE1-4 do not appear to target peptides containing N-terminal E. At the same time all four isoforms, to a various degree, show prominent reactivity with the peptides bearing N-terminal C. Even more strikingly, ATE1-1, unlike any other ATE1 isoforms, appears to be reactive with additional N-terminal sites not seen with other ATE1 isoforms, including Q and, weakly, H. Thus, it appears that N-terminal target site specificity of ATE1-1 may be broader than other ATE1 isoforms and potentially include non-canonical N-terminal residues. The four ATE1 isoforms also show different reactivity with the peptides bearing side chain target sites. In the case of ATE1-1 and ATE1-2, the signal with these peptides containing side chain target sites is substantially lower or absent compared to the peptides containing favorable N-terminal target sites. Side chain arginylation of one of these peptides with ATE1-2 in solution. It appears likely that the peptide array format is unfavorable for side chain targeting by these ATE1 isoforms. Isozyme ATE1-1 catalyzes arginylation of non-canonical residues. Identification of the arginylation-favorable sequence motif
-
-
-
additional information
?
-
usage of DD-bta15-GFP assay for an 'in-lysate' reaction to examine arginylation activity in cell extracts
-
-
-
additional information
?
-
-
usage of DD-bta15-GFP assay for an 'in-lysate' reaction to examine arginylation activity in cell extracts
-
-
-
additional information
?
-
N-terminal Asp, Glu, or oxidized Cys on peptides and proteins are ATE substrates
-
-
-
additional information
?
-
N-terminal Asp, Glu, or oxidized Cys on peptides and proteins are ATE substrates
-
-
-
additional information
?
-
the enzyme interacts with sHSP17.2a, an Hsp20 class I chaperone
-
-
-
additional information
?
-
-
the enzyme interacts with sHSP17.2a, an Hsp20 class I chaperone
-
-
-
additional information
?
-
N-terminal Asp, Glu, or oxidized Cys on peptides and proteins are ATE substrates
-
-
-
additional information
?
-
-
substrates may reach the cytosol by retro-translocation from the endoplasmic reticulum and then be arginylated
-
-
?
additional information
?
-
-
interaction of enzyme and N-terminal domain of topoisomerase II. Role in Ate1 in modulating the level of topoisomerase through the cell cycle
-
-
?
additional information
?
-
-
usage of DD-bta15-GFP assay for an 'in-lysate' reaction to examine arginylation activity in cell extracts
-
-
-
additional information
?
-
-
usage of DD-bta15-GFP assay for an 'in-lysate' reaction to examine arginylation activity in cell extracts
-
-
-
additional information
?
-
N-terminal Asp, Glu, or oxidized Cys on peptides and proteins are ATE substrates
-
-
-
additional information
?
-
N-terminal Asp, Glu, or oxidized Cys on peptides and proteins are ATE substrates
-
-
-
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
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
L-Arg-tRNA + apolipoprotein A-I
tRNAArg + L-Arg-[apolipoprotein A-I]
-
-
-
-
?
L-Arg-tRNAArg + alpha-1-antitrypsin
tRNAArg + L-Arg-[alpha-1-antitrypsin]
-
-
-
-
?
L-Arg-tRNAArg + apolipoprotein E
tRNAArg + L-Arg-[apolipoprotein E]
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?
L-Arg-tRNAArg + contrapsin-like protease inhibitor-3
tRNAArg + L-Arg-[contrapsin-like protease inhibitor-3]
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-
-
-
?
L-Arg-tRNAArg + glucose-related protein 78
tRNAArg + L-Arg-[glucose-related protein 78]
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-
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?
L-Arg-tRNAArg + protein-disulfide isomerase
tRNAArg + L-Arg-[protein-disulfide isomerase]
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-
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-
?
L-arginyl-tRNAArg + alpha-synuclein
tRNAArg + L-arginyl-[alpha-synuclein]
alpha-syn is arginylated in vitro and in vivo
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?
L-arginyl-tRNAArg + BiP/GRP78 protein
tRNAArg + L-arginyl-[BiP/GRP78 protein]
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?
L-arginyl-tRNAArg + calreticulin
tRNAArg + L-arginyl-[calreticulin]
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-
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?
L-arginyl-tRNAArg + ERF-VII peptide
tRNAArg + L-arginyl-[ERF-VII peptide]
after N-terminal Cys-sulfinic acid formation on ERF-VII peptide through plant cysteine oxidase. An ERF-VII peptide with an N-terminal Gly does not accept Arg, whereas an N-terminal Asp accepts Arg, independent of the presence of PCO1 or 4. A peptide comprising an N-terminal Cys-sulfonic acid is also shown to be a substrate for ATE1, again independent of the presence of PCO1 or 4. Proposed arginylation requirements for the Arg/Cys branch of the N-end rule pathway
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?
L-arginyl-tRNAArg + protein disulfide isomerase
tRNAArg + L-arginyl-[protein disulfide isomerase]
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?
L-arginyl-tRNAArg + acceptor protein
tRNAArg + L-arginyl-[acceptor protein]
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?
L-arginyl-tRNAArg + acceptor protein
tRNAArg + L-arginyl-[acceptor protein]
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?
L-arginyl-tRNAArg + acceptor protein
tRNAArg + L-arginyl-[acceptor protein]
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?
L-arginyl-tRNAArg + acceptor protein