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Information on EC 2.4.2.30 - NAD+ ADP-ribosyltransferase and Organism(s) Drosophila melanogaster and UniProt Accession P35875

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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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This record set is specific for:
Drosophila melanogaster
UNIPROT: P35875
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Word Map
The taxonomic range for the selected organisms is: Drosophila melanogaster
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
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193-kDa vault protein
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adenosine diphosphate ribosyltransferase
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ADP-ribosyltransferase
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ADP-ribosyltransferase (polymerizing)
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ADPRT
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C3 exoenzyme
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exoenzyme C3
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exoenzyme S
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msPARP
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NAD(+) ADP-ribosyltransferase
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NAD+:ADP-ribosyltransferase (polymerizing)
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NAD-protein ADP-ribosyltransferase
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pADPRT
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PAR polymerase
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PARP
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PARP-related/IalphaI-related H5/proline-rich
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PH5P
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poly(ADP-ribose) polymerase
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poly(ADP-ribose) synthase
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poly(ADP-ribose) transferase
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poly(ADP-ribosyl)transferase
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poly[ADP-ribose] synthetase
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TANK1
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TANK2
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Tankyrase-like protein
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Tankyrase-related protein
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TRF1-interacting ankyrin-related ADP-ribose polymerase
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VPARP
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REACTION TYPE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
pentosyl group transfer
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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
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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
NAD+ + (ADP-D-ribosyl)n-acceptor
nicotinamide + (ADP-D-ribosyl)n+1-acceptor
show the reaction diagram
additional information
?
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transcriptional regulation mechanism, overview
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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
NAD+ + (ADP-D-ribosyl)n-acceptor
nicotinamide + (ADP-D-ribosyl)n+1-acceptor
show the reaction diagram
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poly(ADP-ribosyl)ation, i.e. PARylation, plays diverse roles in many molecular and cellular processes, including DNA damage detection and repair, chromatin modification, transcription, cell death pathways, insulator function, and mitotic apparatus function, connections between nuclear NAD+ metabolism and nuclear signaling through PARP-1, physiologic functions, detailed overview, synthesis and degradation of PAR on an acceptor protein, pathway overview, the enzyme is involved in regulation of the steady-state levels of PAR
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?
additional information
?
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transcriptional regulation mechanism, overview
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?
ORGANISM
COMMENTARY hide
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
LOCALIZATION
ORGANISM
UNIPROT
COMMENTARY hide
GeneOntology No.
LITERATURE
SOURCE
GENERAL INFORMATION
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
malfunction
disruption of PARP1 enzymatic activity causes nucleolar disintegration and aberrant localization of nucleolar-specific proteins. PARP1 mutants have increased accumulation of rRNA intermediates and a decrease in ribosome levels
UNIPROT
ENTRY NAME
ORGANISM
NO. OF AA
NO. OF TRANSM. HELICES
MOLECULAR WEIGHT[Da]
SOURCE
SEQUENCE
LOCALIZATION PREDICTION?
PARP_DROME
994
0
113792
Swiss-Prot
other Location (Reliability: 1)
PROTEIN VARIANTS
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
additional information
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phenotypes of isozyme-deficient mutant mice, overview
CLONED (Commentary)
ORGANISM
UNIPROT
LITERATURE
trancriptional regulation, overview
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REF.
AUTHORS
TITLE
JOURNAL
VOL.
PAGES
YEAR
ORGANISM (UNIPROT)
PUBMED ID
SOURCE
Kim, M.Y.; Zhang, T.; Kraus, W.L.
Poly(ADP-ribosyl)ation by PARP-1: PAR-laying NAD+ into a nuclear signal
Genes Dev.
19
1951-1967
2005
Drosophila melanogaster, Mus musculus
Manually annotated by BRENDA team
Boamah, E.; Kotova, E.; Garabedian, M.; Jarnik, M.; Tulin, A.
Poly(ADP-ribose) polymerase 1 (PARP-1) regulates ribosomal biogenesis in Drosophila nucleoli
PLoS Genet.
8
e1002442
2012
Drosophila melanogaster (P35875)
Manually annotated by BRENDA team