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Information on EC 2.4.2.30 - NAD+ ADP-ribosyltransferase and Organism(s) Homo sapiens and UniProt Accession P09874

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EC Tree
     2 Transferases
         2.4 Glycosyltransferases
             2.4.2 Pentosyltransferases
                2.4.2.30 NAD+ ADP-ribosyltransferase
IUBMB Comments
The ADP-D-ribosyl group of NAD+ is transferred to an acceptor carboxy group on a histone or the enzyme itself, and further ADP-ribosyl groups are transferred to the 2'-position of the terminal adenosine moiety, building up a polymer with an average chain length of 20--30 units.
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Select one or more organisms in this record: ?
This record set is specific for:
Homo sapiens
UNIPROT: P09874
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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
parp, pertussis toxin, parp-1, poly(adp-ribose) polymerase, parp1, poly (adp-ribose) polymerase, poly(adp-ribose) polymerase-1, c3 exoenzyme, adprt, exoenzyme s, more
SYNONYM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
(adenosine diphosphoribose)transferase, nicotinamide adenine dinucleotide-protein
-
-
-
-
193-kDa vault protein
-
-
-
-
2,3,7,8-tetrachlorodibenzo-p-dioxin poly(ADP-ribose) polymerase
-
adenosine diphosphate ribosyltransferase
-
-
-
-
ADP-ribosyltransferase
ADP-ribosyltransferase (polymerizing)
-
-
-
-
ADP-ribosyltransferase 3
-
ADP-ribosyltransferase-1
-
ADPRT
-
-
-
-
ARTD10
ARTD10/PARP10
isoform
ARTD11
-
-
ARTD7/PARP15
isoform
ARTD8
-
-
B aggressive lymphoma protein 2
-
C3 exoenzyme
-
-
-
-
diphtheria toxin-like ADP-ribosyltranferase
-
exoenzyme C3
-
-
-
-
exoenzyme S
-
-
-
-
mono(ADP-ribosyl) transferase
-
-
mono-ADP-ribosyltransferase
msPARP
-
-
-
-
NAD(+) ADP-ribosyltransferase
-
-
-
-
NAD+:ADP-ribosyltransferase (polymerizing)
-
-
-
-
NAD-protein ADP-ribosyltransferase
-
-
-
-
pADPRT
-
-
-
-
PARP
-
-
-
-
PARP-related/IalphaI-related H5/proline-rich
-
-
-
-
PARP14
-
-
PH5P
-
-
-
-
poly (ADP-ribose) polymerase-1
-
-
poly(ADP-ribose) polymerase
-
-
-
-
poly(ADP-ribose) polymerase family member 11
-
-
poly(ADP-ribose) polymerase-1
-
-
poly(ADP-ribose) polymerase-11
-
-
poly(ADP-ribose) synthase
-
-
-
-
poly(ADP-ribose) transferase
-
-
-
-
poly(ADP-ribosyl)transferase
-
-
-
-
poly[ADP-ribose] synthetase
-
-
-
-
TANK1
-
-
-
-
TANK2
-
-
-
-
tankyrase I
-
Tankyrase-like protein
-
-
-
-
Tankyrase-related protein
-
-
-
-
TRF1-interacting ankyrin-related ADP-ribose polymerase
-
TRF1-interacting ankyrin-related ADP-ribose polymerase
-
-
-
-
VPARP
-
-
-
-
additional information
REACTION
REACTION DIAGRAM
COMMENTARY hide
ORGANISM
UNIPROT
LITERATURE
NAD+ + (ADP-D-ribosyl)n-acceptor = nicotinamide + (ADP-D-ribosyl)n+1-acceptor + H+
show the reaction diagram
the pART catalytic domain is found associated in Lego-like fashion with a variety of domains, including nucleic acid-binding, protein-protein interaction, and ubiquitylation domains
NAD+ + (ADP-D-ribosyl)n-acceptor = nicotinamide + (ADP-D-ribosyl)n+1-acceptor + H+
show the reaction diagram
the pART catalytic domain is found associated in Lego-like fashion with a variety of domains, including nucleic acid-binding, protein-protein interaction, and ubiquitylation domains
REACTION TYPE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
pentosyl group transfer
-
-
-
-
PATHWAY SOURCE
PATHWAYS
SYSTEMATIC NAME
IUBMB Comments
NAD+:poly(ADP-D-ribosyl)-acceptor ADP-D-ribosyl-transferase
The ADP-D-ribosyl group of NAD+ is transferred to an acceptor carboxy group on a histone or the enzyme itself, and further ADP-ribosyl groups are transferred to the 2'-position of the terminal adenosine moiety, building up a polymer with an average chain length of 20--30 units.
CAS REGISTRY NUMBER
COMMENTARY hide
58319-92-9
-
SUBSTRATE
PRODUCT                       
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate) hide
LITERATURE
(Substrate)
COMMENTARY
(Product) hide
LITERATURE
(Product)
Reversibility
r=reversible
ir=irreversible
?=not specified
NAD+ + (ADP-D-ribosyl)n-acceptor
nicotinamide + (ADP-D-ribosyl)n+1-acceptor
show the reaction diagram
-
-
-
?
NAD+ + (ADP-D-ribosyl)n-acceptor
nicotinamide + (ADP-D-ribosyl)n+1-acceptor
show the reaction diagram
NAD+ + (ADP-D-ribosyl)n-acceptor
nicotinamide + (ADP-D-ribosyl)n+1-acceptor + H+
show the reaction diagram
NAD+ + (ADP-D-ribosyl)n-aryl hydrocarbon receptor
nicotinamide + (ADP-D-ribosyl)n+1-aryl hydrocarbon receptor + H+
show the reaction diagram
-
-
-
?
NAD+ + (ADP-D-ribosyl)n-beta-transducin repeat-containing protein
nicotinamide + (ADP-D-ribosyl)n+1-beta-transducin repeat-containing protein + H+
show the reaction diagram
-
-
-
-
?
NAD+ + (ADP-D-ribosyl)n-NEMO protein
nicotinamide + (ADP-D-ribosyl)n+1-NEMO protein + H+
show the reaction diagram
the enzyme prevents poly-ubiquitination of NEMO protein
-
-
?
NAD+ + (ADP-D-ribosyl)n-peptide LL-37
nicotinamide + (ADP-D-ribosyl)n+1-peptide LL-37 + H+
show the reaction diagram
up to four of the five arginine residues present in peptide LL-37 can be ADP-ribosylated on the same peptide when incubated at a high NAD concentration
-
-
?
NAD+ + (ADP-D-ribosyl)n-serine/arginine-rich protein-specific kinase 2
nicotinamide + (ADP-D-ribosyl)n+1-serine/arginine-rich protein-specific kinase 2 + H+
show the reaction diagram
-
-
-
?
NAD+ + histone H1
nicotinamide + (ADP-D-ribosyl)-histone H1
show the reaction diagram
-
-
-
-
?
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
NAD+ + (ADP-D-ribosyl)n-acceptor
nicotinamide + (ADP-D-ribosyl)n+1-acceptor
show the reaction diagram
-
-
-
?
NAD+ + (ADP-D-ribosyl)n-acceptor
nicotinamide + (ADP-D-ribosyl)n+1-acceptor
show the reaction diagram
-
-
-
?
NAD+ + (ADP-D-ribosyl)n-acceptor
nicotinamide + (ADP-D-ribosyl)n+1-acceptor + H+
show the reaction diagram
NAD+ + (ADP-D-ribosyl)n-aryl hydrocarbon receptor
nicotinamide + (ADP-D-ribosyl)n+1-aryl hydrocarbon receptor + H+
show the reaction diagram
-
-
-
?
NAD+ + (ADP-D-ribosyl)n-beta-transducin repeat-containing protein
nicotinamide + (ADP-D-ribosyl)n+1-beta-transducin repeat-containing protein + H+
show the reaction diagram
-
-
-
-
?
NAD+ + (ADP-D-ribosyl)n-NEMO protein
nicotinamide + (ADP-D-ribosyl)n+1-NEMO protein + H+
show the reaction diagram
the enzyme prevents poly-ubiquitination of NEMO protein
-
-
?
additional information
?
-
METALS and IONS
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
Ba2+
-
enhances activity
Mg2+
-
enhances both the automodification and poly(ADP-ribosyl)ation of histone H1
Sr2+
-
enhances activity
INHIBITOR
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
(2S)-2-[[3-(4-oxo-3,4-dihydroquinazolin-2-yl)propanoyl]amino]-3-phenylpropanamide
-
(beta,beta-dimethylacryl)shikonin
64% inhibition at 0.01 mM
3-(4-oxo-3,4-dihydroquinazolin-2-yl)-N-[(1R)-1-(pyridin-2-yl)ethyl]propanamide
-
3-(4-oxo-3,4-dihydroquinazolin-2-yl)-N-[(1R)-1-phenylethyl]propanamide
-
3-(4-oxo-3,4-dihydroquinazolin-2-yl)-N-[(1S)-1-(pyridin-2-yl)ethyl]propanamide
-
3-(4-oxo-3,4-dihydroquinazolin-2-yl)-N-[(1S)-1-phenylethyl]propanamide
-
3-(4-oxo-3,4-dihydroquinazolin-2-yl)-N-[(1S)-1-phenylpropyl]propanamide
-
3-(4-oxo-3,4-dihydroquinazolin-2-yl)-N-[1-(4-sulfamoylphenyl)ethyl]propanamide
-
3-(4-oxo-3,4-dihydroquinazolin-2-yl)-N-[1-(pyridin-2-yl)ethyl]propanamide
-
3-aminobenzamide
3-aminobenzoic acid
-
1 mM, 12% inhibition
4,4'-(methylmino)dibenzamide
26% inhibition at 0.01 mM
4,4'-thiodibenzamide
30% inhibition at 0.01 mM
4-(2-fluorophenoxy)benzamide
-
4-(2-phenoxyethoxy)benzamide
-
4-(4-aminophenoxy)benzamide
-
4-(4-carbamoylphenoxy)benzoic acid
-
4-(4-formylphenoxy)benzamide
-
4-(4-hydroxyphenoxy)benzamide
-
4-(4-methoxyphenoxy)benzamide
-
4-(4-nitrobenzoyl)benzamide
24% inhibition at 0.01 mM
4-(benzyloxy)benzamide
-
4-(pyridin-2-yloxy)benzamide
49% inhibition at 0.01 mM
4-butoxybenzamide
-
4-carbamoylphenyl benzoate
-
4-ethoxybenzamide
-
4-hydroxybenzamide
27% inhibition at 0.01 mM
4-methoxybenzamide
-
4-phenoxybenzamide
-
4-[(2-bromophenyl)methoxy]benzamide
-
4-[(2-fluorophenyl)methoxy]benzamide
-
4-[(3,5-dimethylphenyl)methoxy]benzamide
-
4-[(3-bromophenyl)methoxy]benzamide
-
4-[(3-fluorophenyl)methoxy]benzamide
-
4-[(4-cyanophenyl)thio]benzamide
16% inhibition at 0.01 mM
4-[(4-fluorophenyl)methoxy]benzamide
-
4-[(4-methylphenyl)methoxy]benzamide
-
4-[(naphthalen-1-yl)methoxy]benzamide
-
4-[(propan-2-yl)oxy]benzamide
-
4-[(pyridin-2-yl)methoxy]benzamide
-
4-[1-[4-(propan-2-yl)phenyl]ethoxy]benzamide
16% inhibition at 0.01 mM
4-[4-(1-aminoethenyl)phenoxy]benzamide
4-[[4-(aminocarbonyl)benzyl]oxy]benzamide
-
bergapten
69% inhibition at 0.01 mM
Cu2+
-
-
deoxyshikonin
67% inhibition at 0.01 mM
EB-47
i.e. 5'-deoxy-5'-[4-[2-[(2,3-dihydro-1-oxo-1H-isoindol-4-yl)amino]-2-oxoethyl]-1-piperazinyl]-5'-oxoadenosine dihydrochloride
embelin
57% inhibition at 0.01 mM
gambogic acid
75% inhibition at 0.01 mM
gossypol
75% inhibition at 0.01 mM
Hg2+
-
-
menadione
55% inhibition at 0.01 mM
methyl (2S)-2-[[3-(4-oxo-3,4-dihydroquinazolin-2-yl)propanoyl]amino]-3-phenylpropanoate
-
myricetin
78% inhibition at 0.01 mM
N-[(1R)-2,3-dihydro-1H-inden-1-yl]-3-(4-oxo-3,4-dihydroquinazolin-2-yl)propanamide
-
N-[(1S)-2,3-dihydro-1H-inden-1-yl]-3-(4-oxo-3,4-dihydroquinazolin-2-yl)propanamide
-
N-[(2S)-1-hydroxy-3-phenylpropan-2-yl]-3-(4-oxo-3,4-dihydroquinazolin-2-yl)propanamide
-
N-[(2S)-1-hydroxybutan-2-yl]-3-(4-oxo-3,4-dihydroquinazolin-2-yl)propanamide
-
N-[(2S)-1-hydroxypropan-2-yl]-3-(4-oxo-3,4-dihydroquinazolin-2-yl)propanamide
-
N-[1-[4-(1H-imidazol-1-yl)phenyl]ethyl]-3-(4-oxo-3,4-dihydroquinazolin-2-yl)propanamide
-
nicotinamide
-
1 mM, 93% inhibition
olaparib
PCMB
-
complete
phenantridinone
i.e. 6(5H)-phenantridinone
Plumbagin
67% inhibition at 0.01 mM
rabusertib
-
-
rucaparib
-
-
TIQ-A
i.e. 4H-thieno[2,3-c]isoquinolin-5-one
trimethylpsoralen
61% inhibition at 0.01 mM
VE822
-
-
veliparib
-
-
Zn2+
-
-
ACTIVATING COMPOUND
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
additional information
-
stable expression of the transcription factor tonicity-responsive enhancer/osmotic response element-binding protein, TonEBP/OREBP, clone KIAA0827/amino acids 1-547, in HEK-293 cells increases the expression of the enzyme
-
IC50 VALUE [mM]
INHIBITOR
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
0.0038
(2S)-2-[[3-(4-oxo-3,4-dihydroquinazolin-2-yl)propanoyl]amino]-3-phenylpropanamide
Homo sapiens
pH and temperature not specified in the publication
0.1
3-(4-oxo-3,4-dihydroquinazolin-2-yl)-N-[(1R)-1-(pyridin-2-yl)ethyl]propanamide
Homo sapiens
IC50 above 0.1 mM, pH and temperature not specified in the publication
0.0152
3-(4-oxo-3,4-dihydroquinazolin-2-yl)-N-[(1R)-1-phenylethyl]propanamide
Homo sapiens
pH and temperature not specified in the publication
0.0013
3-(4-oxo-3,4-dihydroquinazolin-2-yl)-N-[(1S)-1-(pyridin-2-yl)ethyl]propanamide
Homo sapiens
pH and temperature not specified in the publication
0.0009
3-(4-oxo-3,4-dihydroquinazolin-2-yl)-N-[(1S)-1-phenylethyl]propanamide
Homo sapiens
pH and temperature not specified in the publication
0.0022
3-(4-oxo-3,4-dihydroquinazolin-2-yl)-N-[(1S)-1-phenylpropyl]propanamide
Homo sapiens
pH and temperature not specified in the publication
0.0144
3-(4-oxo-3,4-dihydroquinazolin-2-yl)-N-[1-(4-sulfamoylphenyl)ethyl]propanamide
Homo sapiens
pH and temperature not specified in the publication
0.0017
4-(2-fluorophenoxy)benzamide
Homo sapiens
pH and temperature not specified in the publication
0.0019
4-(2-phenoxyethoxy)benzamide
Homo sapiens
pH and temperature not specified in the publication
0.0013
4-(4-aminophenoxy)benzamide
Homo sapiens
pH and temperature not specified in the publication
0.00018
4-(4-carbamoylphenoxy)benzoic acid
Homo sapiens
pH and temperature not specified in the publication
0.00071
4-(4-formylphenoxy)benzamide
Homo sapiens
pH and temperature not specified in the publication
0.0018
4-(4-hydroxyphenoxy)benzamide
Homo sapiens
pH and temperature not specified in the publication
0.0014
4-(4-methoxyphenoxy)benzamide
Homo sapiens
pH and temperature not specified in the publication
0.0014
4-(benzyloxy)benzamide
Homo sapiens
pH and temperature not specified in the publication
0.00072
4-butoxybenzamide
Homo sapiens
pH and temperature not specified in the publication
0.0073
4-carbamoylphenyl benzoate
Homo sapiens
pH and temperature not specified in the publication
0.0035
4-ethoxybenzamide
Homo sapiens
pH and temperature not specified in the publication
0.0028
4-methoxybenzamide
Homo sapiens
pH and temperature not specified in the publication
0.0011
4-phenoxybenzamide
Homo sapiens
pH and temperature not specified in the publication
0.0038
4-[(2-bromophenyl)methoxy]benzamide
Homo sapiens
pH and temperature not specified in the publication
0.00023
4-[(2-fluorophenyl)methoxy]benzamide
Homo sapiens
pH and temperature not specified in the publication
0.0045
4-[(3,5-dimethylphenyl)methoxy]benzamide
Homo sapiens
pH and temperature not specified in the publication
0.0022
4-[(3-bromophenyl)methoxy]benzamide
Homo sapiens
pH and temperature not specified in the publication
0.0033
4-[(3-fluorophenyl)methoxy]benzamide
Homo sapiens
pH and temperature not specified in the publication
0.0079
4-[(4-fluorophenyl)methoxy]benzamide
Homo sapiens
pH and temperature not specified in the publication
0.0093
4-[(4-methylphenyl)methoxy]benzamide
Homo sapiens
pH and temperature not specified in the publication
0.0014
4-[(naphthalen-1-yl)methoxy]benzamide
Homo sapiens
pH and temperature not specified in the publication
0.0013
4-[(propan-2-yl)oxy]benzamide
Homo sapiens
pH and temperature not specified in the publication
0.00135
4-[(pyridin-2-yl)methoxy]benzamide
Homo sapiens
pH and temperature not specified in the publication
0.000329 - 0.00033
4-[4-(1-aminoethenyl)phenoxy]benzamide
0.002
4-[[4-(aminocarbonyl)benzyl]oxy]benzamide
Homo sapiens
pH and temperature not specified in the publication
0.00118
EB-47
Homo sapiens
isoform ARDT10, pH and temperature not specified in the publication
0.0022
methyl (2S)-2-[[3-(4-oxo-3,4-dihydroquinazolin-2-yl)propanoyl]amino]-3-phenylpropanoate
Homo sapiens
pH and temperature not specified in the publication
0.1
N-[(1R)-2,3-dihydro-1H-inden-1-yl]-3-(4-oxo-3,4-dihydroquinazolin-2-yl)propanamide
Homo sapiens
IC50 above 0.1 mM, pH and temperature not specified in the publication
0.1
N-[(1S)-2,3-dihydro-1H-inden-1-yl]-3-(4-oxo-3,4-dihydroquinazolin-2-yl)propanamide
Homo sapiens
IC50 above 0.1 mM, pH and temperature not specified in the publication
0.001
N-[(2S)-1-hydroxy-3-phenylpropan-2-yl]-3-(4-oxo-3,4-dihydroquinazolin-2-yl)propanamide
Homo sapiens
pH and temperature not specified in the publication
0.0096
N-[(2S)-1-hydroxybutan-2-yl]-3-(4-oxo-3,4-dihydroquinazolin-2-yl)propanamide
Homo sapiens
pH and temperature not specified in the publication
0.0111
N-[(2S)-1-hydroxypropan-2-yl]-3-(4-oxo-3,4-dihydroquinazolin-2-yl)propanamide
Homo sapiens
pH and temperature not specified in the publication
0.0132
N-[1-[4-(1H-imidazol-1-yl)phenyl]ethyl]-3-(4-oxo-3,4-dihydroquinazolin-2-yl)propanamide
Homo sapiens
pH and temperature not specified in the publication
0.000925 - 0.00204
olaparib
0.000745 - 0.00114
phenantridinone
0.000232
TIQ-A
Homo sapiens
isoform ARDT7, pH and temperature not specified in the publication
SPECIFIC ACTIVITY [µmol/min/mg]
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
0.325
-
-
1.02
-
-
pH OPTIMUM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
8.5
-
reaction with histone in presence of DNA, 0.1 M glycine-NaOH buffer
8.7
-
reaction with histone in presence of DNA, 0.1 M Tris-HCl buffer
ORGANISM
COMMENTARY hide
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
PARP-1
SwissProt
Manually annotated by BRENDA team
GENERAL INFORMATION
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
malfunction
metabolism
physiological function
UNIPROT
ENTRY NAME
ORGANISM
NO. OF AA
NO. OF TRANSM. HELICES
MOLECULAR WEIGHT[Da]
SOURCE
SEQUENCE
LOCALIZATION PREDICTION?
PARP1_HUMAN
1014
0
113084
Swiss-Prot
other Location (Reliability: 2)
PDB
SCOP
CATH
UNIPROT
ORGANISM
MOLECULAR WEIGHT
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
116000
-
1 * 116000, SDS-PAGE
25000
x * 25000, SDS-PAGE
SUBUNIT
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
monomer
-
1 * 116000, SDS-PAGE
CRYSTALLIZATION (Commentary)
ORGANISM
UNIPROT
LITERATURE
in complex with inhibitors, sitting drop vapor diffusion method
PROTEIN VARIANTS
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
G888W
H532A
inactive
I163A
the enzyme shows wild type activity
Y564A
inactive
additional information
PURIFICATION (Commentary)
ORGANISM
UNIPROT
LITERATURE
HisTrap column chromatography
Ni-NTA column chromatography, heparin column chromatography, and gel filtration
CLONED (Commentary)
ORGANISM
UNIPROT
LITERATURE
gene PARP1, chromosomal location 1q41-q42, DNA and amino acid sequence determination, exon compositions, phylogenetic analysis, identification of two subgroups of the family of PARP-like poly(ADP-ribosyl)transferases, depending on the active site residues, overview
expressed in Escherichia coli Rosetta2 (DE3) cells
expressed in Mus musculus
-
expression of the enzyme in HEK-293 cells using a luciferase reporter vector, PARP-1 expression analysis, overview
-
gene PARP11, chromosomal location 12p13.3, DNA and amino acid sequence determination, exon compositions, phylogenetic analysis, identification of two subgroups of the family of PARP-like poly(ADP-ribosyl)transferases, depending on the active site residues, overview
gene PARP14, chromosomal location 3q21.1, DNA and amino acid sequence determination, exon compositions, phylogenetic analysis, identification of two subgroups of the family of PARP-like poly(ADP-ribosyl)transferases, depending on the active site residues, overview
gene PARP16, chromosomal location 15q22.2, DNA and amino acid sequence determination, exon compositions, phylogenetic analysis, identification of two subgroups of the family of PARP-like poly(ADP-ribosyl)transferases, depending on the active site residues, overview
gene PARP2, chromosomal location 14q11.2-q12, DNA and amino acid sequence determination, exon compositions, phylogenetic analysis, identification of two subgroups of the family of PARP-like poly(ADP-ribosyl)transferases, depending on the active site residues, overview
gene PARP3, chromosomal location 3p21.1-22.2, DNA and amino acid sequence determination, exon compositions, phylogenetic analysis, identification of two subgroups of the family of PARP-like poly(ADP-ribosyl)transferases, depending on the active site residues, overview
gene PARP4, chromosomal location 13q11, DNA and amino acid sequence determination, exon compositions, phylogenetic analysis, identification of two subgroups of the family of PARP-like poly(ADP-ribosyl)transferases, depending on the active site residues, overview
gene PARP6, chromosomal location 15q22.23, DNA and amino acid sequence determination, exon compositions, phylogenetic analysis, identification of two subgroups of the family of PARP-like poly(ADP-ribosyl)transferases, depending on the active site residues, overview
gene TNKS1, chromosomal location 8p23.1, DNA and amino acid sequence determination, exon compositions, phylogenetic analysis, identification of two subgroups of the family of PARP-like poly(ADP-ribosyl)transferases, depending on the active site residues, overview
PARP-1, DNA and amino acid sequence determination and analysis of wild-type and mutant genes
-
EXPRESSION
ORGANISM
UNIPROT
LITERATURE
enzyme expression is upregulated by virus infections, including vesicular stomatitis virus, herpes simplex virus-1 and influenza A virus, thus promoting ADP-ribosylation-mediated viral evasion
-
REF.
AUTHORS
TITLE
JOURNAL
VOL.
PAGES
YEAR
ORGANISM (UNIPROT)
PUBMED ID
SOURCE
Ushiro, H.; Yokoyama, Y.; Shizuta, Y.
Purification and characterization of poly (ADP-ribose) synthetase from human placenta
J. Biol. Chem.
262
2352-2357
1987
Homo sapiens
Manually annotated by BRENDA team
Schweiger, M.; Auer, B.; Burtscher, H.J.; Hirsch-Kauffmann, M.; Klocker, H.; Schneider, R.
The Fritz-Lipmann lecture. DNA repair in human cells. Biochemistry of the hereditary diseases Fanconis anaemia and Cockayne syndrome
Eur. J. Biochem.
165
235-242
1987
Homo sapiens
Manually annotated by BRENDA team
Satoh, M.S.; Lindahl, T.
Role of poly(ADP-ribose) formation in DNA repair
Nature
356
356-358
1992
Homo sapiens
Manually annotated by BRENDA team
Lonskaya, I.; Potaman, V.N.; Shlyakhtenko, L.S.; Oussatcheva, E.A.; Lyubchenko, Y.L.; Soldatenkov, V.A.
Regulation of poly(ADP-ribose) polymerase-1 by DNA structure-specific binding
J. Biol. Chem.
280
17076-17083
2005
Homo sapiens
Manually annotated by BRENDA team
Chen, Y.; Schnetz, M.P.; Irarrazabal, C.E.; Shen, R.F.; Williams, C.K.; Burg, M.B.; Ferraris, J.D.
Proteomic identification of proteins associated with the osmoregulatory transcription factor TonEBP/OREBP: functional effects of Hsp90 and PARP-1
Am. J. Physiol. Renal Physiol.
292
F981-F992
2007
Homo sapiens
Manually annotated by BRENDA team
Otto, H.; Reche, P.A.; Bazan, F.; Dittmar, K.; Haag, F.; Koch-Nolte, F.
In silico characterization of the family of PARP-like poly(ADP-ribosyl)transferases (pARTs)
BMC Genomics
6
139
2005
Mus musculus, Homo sapiens (O95271), Homo sapiens (P09874), Homo sapiens (Q2NL67), Homo sapiens (Q460N5), Homo sapiens (Q8N5Y8), Homo sapiens (Q9NR21), Homo sapiens (Q9UGN5), Homo sapiens (Q9UKK3), Homo sapiens (Q9Y6F1)
Manually annotated by BRENDA team
Infante, J.; Sanchez-Juan, P.; Mateo, I.; Rodriguez-Rodriguez, E.; Sanchez-Quintana, C.; Llorca, J.; Fontalba, A.; Terrazas, J.; Oterino, A.; Berciano, J.; Combarros, O.
Poly (ADP-ribose) polymerase-1 (PARP-1) genetic variants are protective against Parkinsons disease
J. Neurol. Sci.
256
68-70
2007
Homo sapiens
Manually annotated by BRENDA team
Meyer-Ficca, M.L.; Ihara, M.; Bader, J.J.; Leu, N.A.; Beneke, S.; Meyer, R.G.
Spermatid head elongation with normal nuclear shaping requires ADP-ribosyltransferase PARP11 (ARTD11) in mice
Biol. Reprod.
92
80
2015
Homo sapiens
Manually annotated by BRENDA team
Venkannagari, H.; Fallarero, A.; Feijs, K.L.; Luescher, B.; Lehtioe, L.
Activity-based assay for human mono-ADP-ribosyltransferases ARTD7/PARP15 and ARTD10/PARP10 aimed at screening and profiling inhibitors
Eur. J. Pharm. Sci.
49
148-156
2013
Homo sapiens (Q460N3), Homo sapiens (Q53GL7), Homo sapiens
Manually annotated by BRENDA team
Picchianti, M.; Russo, C.; Castagnini, M.; Biagini, M.; Soldaini, E.; Balducci, E.
NAD-dependent ADP-ribosylation of the human antimicrobial and immune-modulatory peptide LL-37 by ADP-ribosyltransferase-1
Innate Immun.
21
314-321
2015
Homo sapiens (Q53GL7), Homo sapiens
Manually annotated by BRENDA team
Nicolae, C.M.; Aho, E.R.; Vlahos, A.H.; Choe, K.N.; De, S.; Karras, G.I.; Moldovan, G.L.
The ADP-ribosyltransferase PARP10/ARTD10 interacts with proliferating cell nuclear antigen (PCNA) and is required for DNA damage tolerance
J. Biol. Chem.
289
13627-13637
2014
Homo sapiens (Q53GL7)
Manually annotated by BRENDA team
Lindgren, A.E.; Karlberg, T.; Ekblad, T.; Spjut, S.; Thorsell, A.G.; Andersson, C.D.; Nhan, T.T.; Hellsten, V.; Weigelt, J.; Linusson, A.; Schueler, H.; Elofsson, M.
Chemical probes to study ADP-ribosylation: synthesis and biochemical evaluation of inhibitors of the human ADP-ribosyltransferase ARTD3/PARP3
J. Med. Chem.
56
9556-9568
2013
Homo sapiens (Q9Y6F1), Homo sapiens
Manually annotated by BRENDA team
Verheugd, P.; Forst, A.H.; Milke, L.; Herzog, N.; Feijs, K.L.; Kremmer, E.; Kleine, H.; Luescher, B.
Regulation of NF-kappaB signalling by the mono-ADP-ribosyltransferase ARTD10
Nat. Commun.
4
1683
2013
Homo sapiens (Q53GL7)
Manually annotated by BRENDA team
MacPherson, L.; Tamblyn, L.; Rajendra, S.; Bralha, F.; McPherson, J.; Matthews, J.
2,3,7,8-Tetrachlorodibenzo-p-dioxin poly(ADP-ribose) polymerase (TiPARP, ARTD14) is a mono-ADP-ribosyltransferase and repressor of aryl hydrocarbon receptor transactivation
Nucleic Acids Res.
41
1604-1621
2013
Homo sapiens (Q7Z3E1)
Manually annotated by BRENDA team
Venkannagari, H.; Verheugd, P.; Koivunen, J.; Haikarainen, T.; Obaji, E.; Ashok, Y.; Narwal, M.; Pihlajaniemi, T.; Luescher, B.; Lehtioe, L.
Small-molecule chemical probe rescues cells from mono-ADP-ribosyltransferase ARTD10/PARP10-induced apoptosis and sensitizes cancer cells to DNA damage
Cell Chem. Biol.
23
1251-1260
2016
Homo sapiens (Q53GL7), Homo sapiens
Manually annotated by BRENDA team
Murthy, S.; Desantis, J.; Verheugd, P.; Maksimainen, M.M.; Venkannagari, H.; Massari, S.; Ashok, Y.; Obaji, E.; Nkizinkinko, Y.; Luescher, B.; Tabarrini, O.; Lehtioe, L.
4-(Phenoxy) and 4-(benzyloxy)benzamides as potent and selective inhibitors of mono-ADP-ribosyltransferase PARP10/ARTD10
Eur. J. Med. Chem.
156
93-102
2018
Homo sapiens (Q53GL7), Homo sapiens
Manually annotated by BRENDA team
Guo, T.; Zuo, Y.; Qian, L.; Liu, J.; Yuan, Y.; Xu, K.; Miao, Y.; Feng, Q.; Chen, X.; Jin, L.; Zhang, L.; Dong, C.; Xiong, S.; Zheng, H.
ADP-ribosyltransferase PARP11 modulates the interferon antiviral response by mono-ADP-ribosylating the ubiquitin E3 ligase beta-TrCP
Nat. Microbiol.
4
1872-1884
2019
Homo sapiens
Manually annotated by BRENDA team
Dhoonmoon, A.; Schleicher, E.M.; Clements, K.E.; Nicolae, C.M.; Moldovan, G.L.
Genome-wide CRISPR synthetic lethality screen identifies a role for the ADP-ribosyltransferase PARP14 in DNA replication dynamics controlled by ATR
Nucleic Acids Res.
48
7252-7264
2020
Homo sapiens
Manually annotated by BRENDA team