2.3.2.8: arginyltransferase
This is an abbreviated version!
For detailed information about arginyltransferase, go to the full flat file.
Word Map on EC 2.3.2.8
-
2.3.2.8
-
arginylation
-
2.5.1.18
-
rx:glutathione
-
rx
-
n-degrons
-
polyubiquitylates
-
medicine
-
agriculture
- 2.3.2.8
-
arginylation
-
2.5.1.18
-
rx:glutathione
- rx
-
n-degrons
-
polyubiquitylates
- medicine
- agriculture
Reaction
Synonyms
Arg-transferase, Arg-tRNA transferase, Arg-tRNA-protein transferase, Arg-tRNA-proteintransferase, arginyl 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 1, arginyl-tRNA-protein transferase, arginyl-tRNA-protein transferase 1, arginyl-tRNA:protein arginyltransferase, arginyltransferase, arginyltransferase 1, ATE, Ate1, ATE1-1, ATE1-2, Ate1-3, Ate1-4, ATE1-encoded R-transferase, DdAte1, L-arginyltransferase, R-transferase
ECTree
2.3.2.8 arginyltransferaseAdvanced search results
results (
results (Substrates Products
Substrates Products on EC 2.3.2.8 - arginyltransferase
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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
-
-
-
