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Information on EC 2.3.2.8 - arginyltransferase and Organism(s) Homo sapiens and UniProt Accession O95260

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EC Tree
     2 Transferases
         2.3 Acyltransferases
             2.3.2 Aminoacyltransferases
                2.3.2.8 arginyltransferase
IUBMB 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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This record set is specific for:
Homo sapiens
UNIPROT: O95260
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Word Map
The taxonomic range for the selected organisms is: Homo sapiens
The expected taxonomic range for this enzyme is: Eukaryota, Bacteria, Archaea
Synonyms
arginyltransferase, r-transferase, arginyl-trna-protein transferase, arginyl-trna protein transferase, arg-transferase, arginyltransferase 1, arginyl transferase, arginyl-transferase, arginyl-trna:protein arginyltransferase, ate1-1, more
SYNONYM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
Arg-tRNA-protein transferase
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arginyl-tRNA--protein transferase 1
UniProt
arginyltransferase 1
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ATE1-encoded R-transferase
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arginyl tRNA transferase
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-
-
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arginyl-transfer ribonucleate-protein aminoacyltransferase
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-
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arginyl-transfer ribonucleate-protein transferase
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-
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arginyl-tRNA protein transferase
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-
-
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arginyltransferase
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Ate1
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L-arginyltransferase
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-
-
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R-transferase
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-
-
-
REACTION TYPE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
Acyl group transfer
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-
-
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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.
CAS REGISTRY NUMBER
COMMENTARY hide
37257-24-2
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SUBSTRATE
PRODUCT                       
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate) hide
LITERATURE
(Substrate)
COMMENTARY
(Product) hide
LITERATURE
(Product)
Reversibility
r=reversible
ir=irreversible
?=not specified
L-arginyl-tRNAArg + acceptor protein
tRNAArg + L-arginyl-[acceptor protein]
show the reaction diagram
-
-
-
?
L-arginyl-tRNAArg + protein
tRNAArg + L-arginyl-[protein]
show the reaction diagram
-
-
-
?
L-arginyl-tRNAArg + protein
tRNAArg + L-arginyl-[protein]
show the reaction diagram
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-
-
-
?
additional information
?
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NATURAL SUBSTRATE
NATURAL PRODUCT
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate) hide
LITERATURE
(Substrate)
COMMENTARY
(Product) hide
LITERATURE
(Product)
REVERSIBILITY
r=reversible
ir=irreversible
?=not specified
L-arginyl-tRNAArg + acceptor protein
tRNAArg + L-arginyl-[acceptor protein]
show the reaction diagram
-
-
-
?
L-arginyl-tRNAArg + protein
tRNAArg + L-arginyl-[protein]
show the reaction diagram
-
-
-
?
L-arginyl-tRNAArg + protein
tRNAArg + L-arginyl-[protein]
show the reaction diagram
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-
-
-
?
additional information
?
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the Arg/N-end rule-mediated autophagic flux regulator might be a direct substrate of ATE1, rather than UBR1 or UBR2
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-
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INHIBITOR
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
homocysteine-responsive endoplasmic reticlulum protein
i.e. HERP, a key inhibitor of the turnover and N-terminal arginylation of molecular chaperone BiP. HERP is a 43-kDa endoplasmic reticlulum (ER) membrane-integrated protein that is an essential component of ER-associated protein degradation
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additional information
para-chloroamphetamine, PCA, a specific inhibitor of the arginylation branch of the pathway (Arg/N-end rule pathway). PCA significantly alters various biological pathways, including cellular responses to stress, nutrient, and DNA damage, which are also closely involved in modulation of autophagic responses. Treatment with para-chloroamphetamine (PCA) delays the fusion of autophagosomes with lysosomes and leads to the accumulation of autophagic markers. Analysis of PCA effects in wild-type and mutant (ubr1-/- ubr2-/-) HeLa cells. The direct targets of PCA are UBR1 and UBR2 proteins, not ATE1, an upstream component of the Arg/N-end rule pathway
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ORGANISM
COMMENTARY hide
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
SOURCE TISSUE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
SOURCE
LOCALIZATION
ORGANISM
UNIPROT
COMMENTARY hide
GeneOntology No.
LITERATURE
SOURCE
GENERAL INFORMATION
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
evolution
eukaryotic systems including Saccharomyces cerevisiae (budding yeast), mouse cells, and human cells, all contain the evolutionarily conserved ATE1 gene
malfunction
metabolism
physiological function
physiological function
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the enzyme is essential for tumor suppression and also participates in suppression of metastatic growth
UNIPROT
ENTRY NAME
ORGANISM
NO. OF AA
NO. OF TRANSM. HELICES
MOLECULAR WEIGHT[Da]
SOURCE
SEQUENCE
LOCALIZATION PREDICTION?
ATE1_HUMAN
518
0
59090
Swiss-Prot
other Location (Reliability: 1)
PROTEIN VARIANTS
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
additional information
CLONED (Commentary)
ORGANISM
UNIPROT
LITERATURE
gene ate1, single copy gene
EXPRESSION
ORGANISM
UNIPROT
LITERATURE
Ate1 and arginylation are upregulated during stress and are responsible for cell death, stress is caused by e.g. H2O2, CdCl2, heat, high salt, or staurosporine, overview
the enzyme is downregulated in several types of human cancer samples at the protein level
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APPLICATION
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
medicine
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arginyltransferase inversely correlates with metastases in human cancers and patient survival
REF.
AUTHORS
TITLE
JOURNAL
VOL.
PAGES
YEAR
ORGANISM (UNIPROT)
PUBMED ID
SOURCE
Kwon, Y.T.; Kashina, A.S.; Varshavsky, A.
Alternative splicing results in differential expression, activity, and localization of the two forms of arginyl-tRNA-protein transferase, a component of the N-end rule pathway
Mol. Cell. Biol.
19
182-193
1999
Homo sapiens (O95260), Homo sapiens, Mus musculus (Q9Z2A5), Mus musculus
Manually annotated by BRENDA team
Rai, R.; Zhang, F.; Colavita, K.; Leu, N.A.; Kurosaka, S.; Kumar, A.; Birnbaum, M.D.; Gyorffy, B.; Dong, D.W.; Shtutman, M.; Kashina, A.
Arginyltransferase suppresses cell tumorigenic potential and inversely correlates with metastases in human cancers
Oncogene
35
4058-4068
2016
Homo sapiens
Manually annotated by BRENDA team
Jiang, Y.; Lee, J.; Lee, J.; Lee, J.; Kim, J.; Choi, W.; Yoo, Y.; Cha-Molstad, H.; Kim, B.; Kwon, Y.; Noh, S.; Kim, K.; Lee, M.
The arginylation branch of the N-end rule pathway positively regulates cellular autophagic flux and clearance of proteotoxic proteins
Autophagy
12
2197-2212
2016
Homo sapiens (O95260), Mus musculus (Q9Z2A5)
Manually annotated by BRENDA team
Kumar, A.; Birnbaum, M.; Patel, D.; Morgan, W.; Singh, J.; Barrientos, A.; Zhang, F.
Posttranslational arginylation enzyme Ate1 affects DNA mutagenesis by regulating stress response
Cell Death Dis.
7
e2378
2016
Homo sapiens (O95260), Homo sapiens, Mus musculus (Q9Z2A5), Mus musculus, Saccharomyces cerevisiae, Saccharomyces cerevisiae BY4741
Manually annotated by BRENDA team
Shim, S.M.; Choi, H.R.; Sung, K.W.; Lee, Y.J.; Kim, S.T.; Kim, D.; Mun, S.R.; Hwang, J.; Cha-Molstad, H.; Ciechanover, A.; Kim, B.Y.; Kwon, Y.T.
The endoplasmic reticulum-residing chaperone BiP is short-lived and metabolized through N-terminal arginylation
Sci. Signal.
11
eaan0630
2018
Homo sapiens (O95260)
Manually annotated by BRENDA team