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Information on EC 2.4.2.31 - NAD+-protein-arginine ADP-ribosyltransferase and Organism(s) Homo sapiens

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EC Tree
     2 Transferases
         2.4 Glycosyltransferases
             2.4.2 Pentosyltransferases
                2.4.2.31 NAD+-protein-arginine ADP-ribosyltransferase
IUBMB Comments
Protein mono-ADP-ribosylation is a reversible post-translational modification that plays a role in the regulation of cellular activities . Arginine residues in proteins act as acceptors. Free arginine, agmatine [(4-aminobutyl)guanidine], arginine methyl ester and guanidine can also do so. The enzyme from some, but not all, species can also use NADP+ as acceptor (giving rise to Nomega-[(2'-phospho-ADP)-D-ribosyl]-protein-L-arginine as the product), but more slowly [1,5]. The enzyme catalyses the NAD+-dependent activation of EC 4.6.1.1, adenylate cyclase. Some bacterial enterotoxins possess similar enzymic activities. (cf. EC 2.4.2.36 NAD+---diphthamide ADP-ribosyltransferase).
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Homo sapiens
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Word Map
The taxonomic range for the selected organisms is: Homo sapiens
The enzyme appears in selected viruses and cellular organisms
Synonyms
at1, at2, iota toxin, rt6.1, rt6.2, mono(adp-ribosyl)transferase, arginine-specific adp-ribosyltransferase, nad:arginine adp-ribosyltransferase, arginine-specific mono-adp-ribosyltransferase, xopai, more
SYNONYM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
(adenosine diphosphoribose)transferase, nicotinamide adenine dinucleotide-arginine
-
-
-
-
ADP-ribosyl-acceptor hydrolase 1
-
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ADP-ribosyltransferase
ADPRT
-
-
-
-
alloantigen Rt6.1
-
-
-
-
alloantigen Rt6.2
-
-
-
-
arginine ADP-ribosyltransferase 1
-
-
arginine specific ADP-ribosyltransferase
-
-
-
-
arginine specific mono-ADP-ribosyltransferase
-
-
-
-
arginine-specific adenosine diphosphate ribosyltransferase 1
-
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arginine-specific ADP-ribosyltransferase
-
-
arginine-specific mono-ADP-ribosyltransferase
ARH1
-
-
ART1
-
-
ART4
-
-
ARTD15/PARP16
-
AT1
-
-
-
-
AT2
-
-
-
-
Dombrock blood group carrier molecule
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-
-
-
mono(ADP-ribosyl)transferase
-
-
-
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mono-ADP-ribosyl-arginine hydrolase
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-
mono-ADP-ribosyltransferase
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NAD(P)+-arginine ADP-ribosyltransferase
-
-
-
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NAD+:arginine ADP-ribosyltransferase
-
-
-
-
NAD+:arginine ecto-mono(ADP-ribosyl)transferase
-
-
-
-
NAD+:L-arginine ADP-D-ribosyltransferase
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-
-
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NAD-arginine ADP-ribosyltransferase
-
-
-
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NAD-arginine mono-ADP-ribosyltransferase B
-
-
-
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NAD-dependent ADPribosyltransferase
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-
-
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NAD:arginine ADP-ribosyltransferase B
-
-
-
-
PARP16/ARTD15
-
RT6
-
-
-
-
RT6.1
-
-
-
-
RT6.2
-
-
-
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T-cell surface protein Rt6.1
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-
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T-cell surface protein Rt6.2
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-
-
-
REACTION TYPE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
pentosyl group transfer
-
-
-
-
SYSTEMATIC NAME
IUBMB Comments
NAD+:protein-L-arginine ADP-D-ribosyltransferase
Protein mono-ADP-ribosylation is a reversible post-translational modification that plays a role in the regulation of cellular activities [4]. Arginine residues in proteins act as acceptors. Free arginine, agmatine [(4-aminobutyl)guanidine], arginine methyl ester and guanidine can also do so. The enzyme from some, but not all, species can also use NADP+ as acceptor (giving rise to Nomega-[(2'-phospho-ADP)-D-ribosyl]-protein-L-arginine as the product), but more slowly [1,5]. The enzyme catalyses the NAD+-dependent activation of EC 4.6.1.1, adenylate cyclase. Some bacterial enterotoxins possess similar enzymic activities. (cf. EC 2.4.2.36 NAD+---diphthamide ADP-ribosyltransferase).
CAS REGISTRY NUMBER
COMMENTARY hide
81457-93-4
-
SUBSTRATE
PRODUCT                       
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate) hide
LITERATURE
(Substrate)
COMMENTARY
(Product) hide
LITERATURE
(Product)
Reversibility
r=reversible
ir=irreversible
?=not specified
agmatine + NAD+
nicotinamide + ?
show the reaction diagram
-
-
-
-
?
basic fibroblast growth factor FGF-2 + NAD+
nicotinamide + ?
show the reaction diagram
-
-
-
-
?
diethylamino-(benzylidineamino)guanidine + NAD+
nicotinamide + ?
show the reaction diagram
-
-
-
-
?
FGF-2 + NAD+
?
show the reaction diagram
-
ADP-ribosylation of FGF-2 may provide an additional level of control of FGF-2 activity
-
-
?
human neutrophil peptide-1 + NAD+
Nomega-(ADP-D-ribosyl)-L-arginine-human neutrophil peptide-1 + nicotinamide
show the reaction diagram
karyopherin-beta1 + NAD+
nicotinamide + ?
show the reaction diagram
-
-
-
?
NAD+ + glucose-regulated protein of 78 kDa/immunoglobulin heavy-chainbinding protein L-arginine
nicotinamide + Nomega-(ADP-D-ribosyl)-glucose-regulated protein of 78 kDa/immunoglobulin heavy-chainbinding protein-L-arginine
show the reaction diagram
-
-
-
?
NAD+ + protein L-arginine
nicotinamide + Nomega-(ADP-D-ribosyl)-protein-L-arginine
show the reaction diagram
-
-
-
-
?
P2X7(k) + NAD+
nicotinamide + ?
show the reaction diagram
-
the P2X7(k) variant is sensitive to activation by ADP-ribosylation whereas the P2X7(a) variant is insensitive
-
-
?
additional information
?
-
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
FGF-2 + NAD+
?
show the reaction diagram
-
ADP-ribosylation of FGF-2 may provide an additional level of control of FGF-2 activity
-
-
?
human neutrophil peptide-1 + NAD+
Nomega-(ADP-D-ribosyl)-L-arginine-human neutrophil peptide-1 + nicotinamide
show the reaction diagram
-
human neutrophil peptide-1, HNP-1, from neutrophil cell surface, ADP-ribosylation of HNP-1 is primarily an activity of ART1 and occurs in inflammatory conditions and disease, lack of modified HNP-1 due to enzyme deficiency in the sputum leads to cystic fibrosis
-
-
?
NAD+ + glucose-regulated protein of 78 kDa/immunoglobulin heavy-chainbinding protein L-arginine
nicotinamide + Nomega-(ADP-D-ribosyl)-glucose-regulated protein of 78 kDa/immunoglobulin heavy-chainbinding protein-L-arginine
show the reaction diagram
-
-
-
?
NAD+ + protein L-arginine
nicotinamide + Nomega-(ADP-D-ribosyl)-protein-L-arginine
show the reaction diagram
-
-
-
-
?
additional information
?
-
-
enzyme is involved in posttranslational modification of proteins
-
-
?
INHIBITOR
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
human neutrophil peptide-1
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substrate inhibition of isozymes ART1 and ART5
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ACTIVATING COMPOUND
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
heparin
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-
NAD+
-
excess
KM VALUE [mM]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
0.1 - 0.29
NAD+
pH OPTIMUM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
7.5
-
assay at
TEMPERATURE OPTIMUM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
30
-
assay at
37
assay at
ORGANISM
COMMENTARY hide
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
SOURCE TISSUE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
SOURCE
-
epithelial cells lining human airways and cells, isozyme ART1, bronchoalveolar lavage fluid
Manually annotated by BRENDA team
additional information
LOCALIZATION
ORGANISM
UNIPROT
COMMENTARY hide
GeneOntology No.
LITERATURE
SOURCE
-
on epithelial cells lining human airways and cells, isozyme ART1
Manually annotated by BRENDA team
GENERAL INFORMATION
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
physiological function
UNIPROT
ENTRY NAME
ORGANISM
NO. OF AA
NO. OF TRANSM. HELICES
MOLECULAR WEIGHT[Da]
SOURCE
SEQUENCE
LOCALIZATION PREDICTION?
NAR1_HUMAN
327
0
36335
Swiss-Prot
Secretory Pathway (Reliability: 1)
NAR3_HUMAN
389
1
43923
Swiss-Prot
Secretory Pathway (Reliability: 1)
NAR4_HUMAN
314
0
35878
Swiss-Prot
Secretory Pathway (Reliability: 3)
NAR5_HUMAN
291
0
32054
Swiss-Prot
Secretory Pathway (Reliability: 1)
A8K6J7_HUMAN
314
0
35865
TrEMBL
Secretory Pathway (Reliability: 3)
Q5IRA6_HUMAN
53
0
5825
TrEMBL
Mitochondrion (Reliability: 3)
A0A0U5FP74_HUMAN
236
0
27448
TrEMBL
other Location (Reliability: 2)
H7C3U2_HUMAN
151
0
17007
TrEMBL
other Location (Reliability: 2)
A0A3P3YW42_HUMAN
236
0
27470
TrEMBL
other Location (Reliability: 2)
E7ER42_HUMAN
174
0
20134
TrEMBL
Secretory Pathway (Reliability: 1)
C3W8I1_HUMAN
236
0
27478
TrEMBL
other Location (Reliability: 2)
Q3KZ27_HUMAN
30
1
3180
TrEMBL
Secretory Pathway (Reliability: 4)
H7C2G2_HUMAN
273
0
31511
TrEMBL
Secretory Pathway (Reliability: 1)
E9PGR5_HUMAN
107
0
12411
TrEMBL
Secretory Pathway (Reliability: 1)
A0A024RDB9_HUMAN
378
1
42742
TrEMBL
Secretory Pathway (Reliability: 1)
H7C1W0_HUMAN
264
0
29075
TrEMBL
other Location (Reliability: 1)
B4DHX3_HUMAN
368
0
41983
TrEMBL
Secretory Pathway (Reliability: 1)
A0A024RCD1_HUMAN
292
0
32155
TrEMBL
Secretory Pathway (Reliability: 1)
A0A166IZP3_HUMAN
236
0
27478
TrEMBL
other Location (Reliability: 2)
A0A3P3YWJ5_HUMAN
236
0
27505
TrEMBL
other Location (Reliability: 2)
Q3KZ25_HUMAN
273
0
31510
TrEMBL
Secretory Pathway (Reliability: 1)
A0A3P3YWC4_HUMAN
236
0
27508
TrEMBL
other Location (Reliability: 2)
Q3KZ26_HUMAN
29
0
3337
TrEMBL
other Location (Reliability: 4)
A0A6C0M8C7_HUMAN
250
0
28566
TrEMBL
Secretory Pathway (Reliability: 3)
A0A3P3YWC5_HUMAN
236
0
27491
TrEMBL
other Location (Reliability: 2)
Q3KZ28_HUMAN
314
0
35818
TrEMBL
Secretory Pathway (Reliability: 3)
D3YNY8_HUMAN
236
0
27535
TrEMBL
other Location (Reliability: 2)
A0A3P3YWF0_HUMAN
236
0
27452
TrEMBL
other Location (Reliability: 2)
C3W8I0_HUMAN
236
0
27479
TrEMBL
other Location (Reliability: 2)
E7ESB3_HUMAN
201
0
23092
TrEMBL
Secretory Pathway (Reliability: 1)
A0A3P3ZJX7_HUMAN
236
0
27504
TrEMBL
other Location (Reliability: 2)
A0A024RDG4_HUMAN
367
1
41515
TrEMBL
Secretory Pathway (Reliability: 1)
E7EX61_HUMAN
129
0
14998
TrEMBL
Secretory Pathway (Reliability: 1)
A1Z625_HUMAN
236
0
27418
TrEMBL
other Location (Reliability: 2)
Q5J1L0_HUMAN
44
0
5055
TrEMBL
-
Q5J1P8_HUMAN
48
0
5556
TrEMBL
-
Q5J1Q0_HUMAN
31
0
3538
TrEMBL
-
PAR16_HUMAN
322
0
36383
Swiss-Prot
-
SIR6_HUMAN
355
0
39119
Swiss-Prot
-
PDB
SCOP
CATH
UNIPROT
ORGANISM
MOLECULAR WEIGHT
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
37000
-
x * 37000, SDS-PAGE
50000
SDS-PAGE
SUBUNIT
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
CRYSTALLIZATION (Commentary)
ORGANISM
UNIPROT
LITERATURE
the crystal structure of human ARTD15/PARP16 is shown. ARTD15 features an alpha-helical domain that packs against its transferase domain without making direct contact with the NAD+-binding crevice or the donor loop
PROTEIN VARIANTS
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
DELTA278-322
a deletion mutant lacking the region encompassing the putative transmembrane domain (aminoacids 278-322) shows a diffuse, cytosolic localization compared with full length ARTD15
K242E
-
displays no activity
Y187R
-
displays no activity
Y187R/K242E
-
double mutant contains the R-S-EXE motif, but displays no activity, thus additional residues besides the intact R-S-EXE motif are involved in catalyzing the enzymatic reaction
CLONED (Commentary)
ORGANISM
UNIPROT
LITERATURE
expressed in Escherichia coli
expressed in HUVEC cells
-
expression Escherichia coli
expression of isozymes ART1, ART3, ART4, ART5, ART2.2 in Escherichia coli, isozyme ART1synthesized in Escherichia coli, glycosylphosphatidylinositol-anchored ART1 released with phosphatidylinositol-specific phospholipase C from transfected NMU cells, or ART1 expressed endogenously on C2C12 myotubes modifiy arginine 14 on HNP-1 with a secondary site on arginine 24
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gene ART3, DNA and amino acid sequence determination and analysis, structural analysis of the untranslated regions, splicing variants differing in the 5'-UTR, genomic organization, expression analysis, recombinant expression in HEK-293T cells
wild-type and mutants cloned into the pcDNA3.1/Zeo (+) plasmid, expression in C-33A cells
-
EXPRESSION
ORGANISM
UNIPROT
LITERATURE
enzyme expression is activated during the endoplasmic reticulum stress response
REF.
AUTHORS
TITLE
JOURNAL
VOL.
PAGES
YEAR
ORGANISM (UNIPROT)
PUBMED ID
SOURCE
Okazaki, I.J.; Kim, H.J.; Moss, J.
Cloning and characterization of a novel membrane-associated lymphocyte NAD:arginine ADP-ribosyltransferase
J. Biol. Chem.
271
22052-22057
1996
Gallus gallus, Oryctolagus cuniculus, Homo sapiens, Mus musculus (P70352), Mus musculus
Manually annotated by BRENDA team
Jones, E.M.; Baird, A.
Cell-surface ADP-ribosylation of fibroblast growth factor-2 by an arginine-specific ADP-ribosyltransferase
Biochem. J.
323
173-177
1997
Bos taurus, Homo sapiens
-
Manually annotated by BRENDA team
Donnelly, L.E.; Rendell, N.B.; Murray, S.; Allport, J.R.; Lo, G.; Kefalas, P.; Taylor, G.W.; MacDermot, J.
Arginine-specific mono(ADP-ribosyl)transferase activity on the surface of human polymorphonuclear neutrophil leukocytes
Biochem. J.
315
635-641
1996
Homo sapiens
-
Manually annotated by BRENDA team
Moss, J.; Balducci, E.; Cavanaugh, E.; Kim, H.J.; Konczalik, P.; Lesma, E.A.; Okazaki, I.J.; Park, M.; Shoemaker, M.; Stevens, L.A.; Zolkiewska, A.
Characterization of NAD:arginine ADP-ribosyltransferases
Mol. Cell. Biochem.
193
109-113
1999
Homo sapiens, Mus musculus, Rattus norvegicus
Manually annotated by BRENDA team
Okazaki, I.J.; Kim, H.J.; Moss, J.
Molecular cloning and characterization of lymphocyte and muscle ADP-ribosyltransferases
Adv. Exp. Med. Biol.
419
129-136
1997
Oryctolagus cuniculus, Homo sapiens, Mus musculus
Manually annotated by BRENDA team
Friedrich, M.; Grahnert, A.; Klein, C.; Tschoep, K.; Engeland, K.; Hauschildt, S.
Genomic organization and expression of the human mono-ADP-ribosyltransferase ART3 gene
Biochim. Biophys. Acta
1759
270-280
2006
Homo sapiens (Q5J1L0), Homo sapiens (Q5J1P8), Homo sapiens (Q5J1Q0)
Manually annotated by BRENDA team
Paone, G.; Stevens, L.A.; Levine, R.L.; Bourgeois, C.; Steagall, W.K.; Gochuico, B.R.; Moss, J.
ADP-ribosyltransferase-specific modification of human neutrophil peptide-1
J. Biol. Chem.
281
17054-17060
2006
Homo sapiens, Mus musculus
Manually annotated by BRENDA team
Grahnert, A.; Richter, S.; Siegert, F.; Berndt, A.; Hauschildt, S.
The orthologue of the "acatalytic" mammalian ART4 in chicken is an arginine-specific mono-ADP-ribosyltransferase
BMC Mol. Biol.
9
86
2008
Homo sapiens, Gallus gallus (B6RDZ5), Gallus gallus
Manually annotated by BRENDA team
Karlberg, T.; Thorsell, A.G.; Kallas, A.; Schueler, H.
Crystal structure of human ADP-ribose transferase ARTD15/PARP16 reveals a novel putative regulatory domain
J. Biol. Chem.
287
24077-24081
2012
Homo sapiens (Q8N5Y8), Homo sapiens
Manually annotated by BRENDA team
Di Paola, S.; Micaroni, M.; Di Tullio, G.; Buccione, R.; Di Girolamo, M.
PARP16/ARTD15 is a novel endoplasmic-reticulum-associated mono-ADP-ribosyltransferase that interacts with, and modifies karyopherin-ss1
PLoS ONE
7
e37352
2012
Homo sapiens (Q8N5Y8), Homo sapiens
Manually annotated by BRENDA team
Schwarz, N.; Drouot, L.; Nicke, A.; Fliegert, R.; Boyer, O.; Guse, A.H.; Haag, F.; Adriouch, S.; Koch-Nolte, F.
Alternative splicing of the N-terminal cytosolic and transmembrane domains of P2X7 controls gating of the ion channel by ADP-ribosylation
PLoS ONE
7
e41269
2012
Homo sapiens
Manually annotated by BRENDA team
Mashimo, M.; Kato, J.; Moss, J.
Structure and function of the ARH family of ADP-ribosyl-acceptor hydrolases
DNA Repair
23
88-94
2014
Homo sapiens
Manually annotated by BRENDA team
Fabrizio, G.; Di Paola, S.; Stilla, A.; Giannotta, M.; Ruggiero, C.; Menzel, S.; Koch-Nolte, F.; Sallese, M.; Di Girolamo, M.
ARTC1-mediated ADP-ribosylation of GRP78/BiP: a new player in endoplasmic-reticulum stress responses
Cell. Mol. Life Sci.
72
1209-1225
2015
Homo sapiens (P52961), Homo sapiens
Manually annotated by BRENDA team
Yang, L.; Xiao, M.; Li, X.; Tang, Y.; Wang, Y.L.
Arginine ADP-ribosyltransferase 1 promotes angiogenesis in colorectal cancer via the PI3K/Akt pathway
Int. J. Mol. Med.
37
734-742
2016
Homo sapiens
Manually annotated by BRENDA team