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InterPro: IPR004102 Poly(ADP-ribose) polymerase, regulatory domain

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Matches:

230 proteins

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Accession List
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Accession

IPR004102 Poly(ADP-ribose)pol_reg_dom

Type

Domain

Signatures Help

Database	ID	Name	Proteins
Gene3D	G3DSA:1.20.142.10	PARP_reg	215
Pfam	PF02877	PARP_reg	170
PROSITE profile	PS51060	PARP_ALPHA_HD	228
SuperFamily	SSF47587	PARP_reg	219
Signatures in BioMart

InterPro Relationships Help

Found in

IPR008288 NAD+ ADP-ribosyltransferase

GO Term annotation Help

Process

GO:0006471 protein amino acid ADP-ribosylation

Function

GO:0003950 NAD+ ADP-ribosyltransferase activity

InterPro annotation

Entry Details in BioMart

Abstract

Poly(ADP-ribose) polymerase catalyses the covalent attachment of ADP-ribose units from NAD+ to itself and to a limited number of other DNA binding proteins, which decreases their affinity for DNA. Poly(ADP-ribose) polymerase is a regulatory component induced by DNA damage. The regulatory domain of the polymerase is almost always associated with the C-terminal catalytic domain (see IPR001290).

This domain consists of a duplication of two helix-loop-helix structural repeats [1].

Structural links Help

PDB - click here

SCOP: a.41.1.1

CATH: 1.20.142.10

Database links Help

Enzyme: EC:2.4.2.30

PROSITE doc: PDOC51059

PANDIT: PF02877

Blocks: IPB004102

Taxonomic coverage Help

Overlapping InterPro entries Help

IPR004102

Numbers of overlapping proteins

Average numbers of overlapping amino acids

Example proteins Help

O88554 Poly [ADP-ribose] polymerase 2

P09874 Poly [ADP-ribose] polymerase 1

P35875 Poly [ADP-ribose] polymerase

Q09525 Poly(ADP-ribose) polymerase pme-2

Q9ZP54 Poly [ADP-ribose] polymerase 1

More proteins

Example Proteins Key

InterPro entry accession number/name and structure databases		Colour code
IPR012317	Poly(ADP-ribose) polymerase, catalytic domain
IPR012982	PADR1
IPR008288	NAD+ ADP-ribosyltransferase
IPR004102	Poly(ADP-ribose) polymerase, regulatory domain
IPR001357	BRCT
IPR001510	Zinc finger, PARP-type
IPR008893	WGR
	SWISS-MODEL
	PDB Chain
	ModBase
	SCOP Domain
	CATH Domain

Publications Open in usermanual
1.	Ruf A, de Murcia G, Schulz GE. Inhibitor and NAD+ binding to poly(ADP-ribose) polymerase as derived from crystal structures and homology modeling. Biochemistry 37 3893-900 1998 [PubMed: 9521710] http://dx.doi.org/10.1021/bi972383s

Additional Reading Open in usermanual
	Simonin F, Hofferer L, Panzeter PL, Muller S, de Murcia G, Althaus FR. The carboxyl-terminal domain of human poly(ADP-ribose) polymerase. Overproduction in Escherichia coli, large scale purification, and characterization. J. Biol. Chem. 268 1993 13454-61 [PubMed: 8390463] http://intl.jbc.org/cgi/content/abstract/268/18/13454
	Ame JC, Spenlehauer C, de Murcia G. The PARP superfamily. Bioessays 26 2004 882-93 [PubMed: 15273990] http://dx.doi.org/10.1002/bies.20085
	Lehtio L, Jemth AS, Collins R, Loseva O, Johansson A, Markova N, Hammarstrom M, Flores A, Holmberg-Schiavone L, Weigelt J, Helleday T, Schuler H, Karlberg T. Structural basis for inhibitor specificity in human poly(ADP-ribose) polymerase-3. J. Med. Chem. 52 2009 3108-11 [PubMed: 19354255] http://dx.doi.org/10.1021/jm900052j
	Nguewa PA, Fuertes MA, Valladares B, Alonso C, Perez JM. Poly(ADP-ribose) polymerases: homology, structural domains and functions. Novel therapeutical applications. Prog. Biophys. Mol. Biol. 88 2005 143-72 [PubMed: 15561303] http://dx.doi.org/10.1016/j.pbiomolbio.2004.01.001
	Hattori K, Kido Y, Yamamoto H, Ishida J, Kamijo K, Murano K, Ohkubo M, Kinoshita T, Iwashita A, Mihara K, Yamazaki S, Matsuoka N, Teramura Y, Miyake H. Rational approaches to discovery of orally active and brain-penetrable quinazolinone inhibitors of poly(ADP-ribose)polymerase. J. Med. Chem. 47 2004 4151-4 [PubMed: 15293985] http://dx.doi.org/10.1021/jm0499256
	Iwashita A, Hattori K, Yamamoto H, Ishida J, Kido Y, Kamijo K, Murano K, Miyake H, Kinoshita T, Warizaya M, Ohkubo M, Matsuoka N, Mutoh S. Discovery of quinazolinone and quinoxaline derivatives as potent and selective poly(ADP-ribose) polymerase-1/2 inhibitors. FEBS Lett. 579 2005 1389-93 [PubMed: 15733846] http://dx.doi.org/10.1016/j.febslet.2005.01.036
	Ruf A, Mennissier de Murcia J, de Murcia G, Schulz GE. Structure of the catalytic fragment of poly(AD-ribose) polymerase from chicken. Proc. Natl. Acad. Sci. U.S.A. 93 1996 7481-5 [PubMed: 8755499] http://dx.doi.org/10.1073/pnas.93.15.7481
	Kinoshita T, Nakanishi I, Warizaya M, Iwashita A, Kido Y, Hattori K, Fujii T. Inhibitor-induced structural change of the active site of human poly(ADP-ribose) polymerase. FEBS Lett. 556 2004 43-6 [PubMed: 14706823] http://dx.doi.org/10.1016/S0014-5793(03)01362-0
	Oliver AW, Ame JC, Roe SM, Good V, de Murcia G, Pearl LH. Crystal structure of the catalytic fragment of murine poly(ADP-ribose) polymerase-2. Nucleic Acids Res. 32 2004 456-64 [PubMed: 14739238] http://dx.doi.org/10.1093/nar/gkh215

InterPro 23.1