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IPR008288 is a Poly [ADP-ribose] polymerase.
<p>Poly(ADP-ribose) synthase and poly(ADP-ribose) polymerase (PARP, also known as ADPRT) catalyse the DNA-dependent covalent attachment of ADP-ribose to various nuclear proteins [[cite:PUB00003624]]. They are used by the eukaryotic cell to cope with numerous environmental and endogenous genotoxic agents that cause DNA strand breaks. PARP plays a role in many cellular processes, including DNA repair, recombination, cell proliferation and death, as well as genomic stability [[cite:PUB00011133]]. The DNA-binding region of the protein contains a pair of zinc finger domains, which have been shown to bind DNA in a zinc-dependent manner [[cite:PUB00011134]]. PARP also contains a BRCT domain involved in cell cycle checkpoint functions responsive to DNA damage [[cite:PUB00001533]], a catalyic domain and a regulatory domain.</p>
This description is obtained from EB-eye REST.
GO predictions are based solely on the InterPro-to-GO mappings published by EMBL-EBI, which are in turn based on the mapping of predicted domains to the InterPro dataset. The InterPro-to-GO mapping was last updated on , while the GO metadata was last updated on .
| GO term | Namespace | Name | Definition | Relationships |
|---|---|---|---|---|
| Molecular function | DNA binding | Any molecular function by which a gene product interacts selectively and non-covalently with DNA (deoxyribonucleic acid). | ||
| Molecular function | NAD+ ADP-ribosyltransferase activity | Catalysis of the reaction: NAD+ + (ADP-D-ribosyl)(n)-acceptor = nicotinamide + (ADP-D-ribosyl)(n+1)-acceptor. | ||
| Cellular component | Nucleus | A membrane-bounded organelle of eukaryotic cells in which chromosomes are housed and replicated. In most cells, the nucleus contains all of the cell's chromosomes except the organellar chromosomes, and is the site of RNA synthesis and processing. In some species, or in specialized cell types, RNA metabolism or DNA replication may be absent. | ||
| Biological process | Protein ADP-ribosylation | The transfer, from NAD, of ADP-ribose to protein amino acids. | ||
| Molecular function | Zinc ion binding | Interacting selectively and non-covalently with zinc (Zn) ions. | ||
| Molecular function | NAD binding | Interacting selectively and non-covalently with nicotinamide adenine dinucleotide, a coenzyme involved in many redox and biosynthetic reactions; binding may be to either the oxidized form, NAD+, or the reduced form, NADH. |
| Transcript | Name | Description | Predicted domains | Domain count |
|---|---|---|---|---|
| – | PREDICTED: poly [ADP]-ribose] gi|502109943|ref|XP_004493762.1| | 37 | ||
| – | Poly [ADP]-ribose] polymerase; TAIR: AT2G31320.1 poly(ADP-ribose) polymerase 2; Swiss-Prot: sp|Q9ZP54|PARP1_ARATH Poly [ADP]-ribose] polymerase 1; TrEMBL-Plants: tr|A0A072U2F3|A0A072U2F3_MEDTR Poly [ADP]-ribose] polymerase; Found in the gene: LotjaGi1g1v0711100 | 46 | ||
| – | Poly [ADP]-ribose] polymerase; TAIR: AT2G31320.1 poly(ADP-ribose) polymerase 2; Swiss-Prot: sp|Q9ZP54|PARP1_ARATH Poly [ADP]-ribose] polymerase 1; TrEMBL-Plants: tr|A0A072U2F3|A0A072U2F3_MEDTR Poly [ADP]-ribose] polymerase; Found in the gene: LotjaGi1g1v0711100 | 45 | ||
| – | Poly [ADP]-ribose] polymerase; TAIR: AT2G31320.1 poly(ADP-ribose) polymerase 2; Swiss-Prot: sp|Q9ZP54|PARP1_ARATH Poly [ADP]-ribose] polymerase 1; TrEMBL-Plants: tr|A0A072U2F3|A0A072U2F3_MEDTR Poly [ADP]-ribose] polymerase; Found in the gene: LotjaGi1g1v0711100 | 45 | ||
| – | Poly [ADP]-ribose] polymerase; TAIR: AT2G31320.1 poly(ADP-ribose) polymerase 2; Swiss-Prot: sp|Q9ZP54|PARP1_ARATH Poly [ADP]-ribose] polymerase 1; TrEMBL-Plants: tr|A0A072U2F3|A0A072U2F3_MEDTR Poly [ADP]-ribose] polymerase; Found in the gene: LotjaGi2g1v0337700 | 45 |
A list of co-occurring predicted domains within the L. japonicus gene space:
| Predicted domain | Source | Observations | Saturation (%) |
|---|---|---|---|
| mobidb-lite | MobiDBLite | 1 | 20.00 |