PARP-3 Protein

Poly (ADP-ribose) polymerase family, member 3

PARP-3 Products

PARP-3 Protein, Recombinant

Molecule	Species	Description	Cat. No
PARP-3	Human	PARP-3/PARP3 Protein, Recombinant, with GST Tag	11190-H20B

PARP-3 cDNA Clone

Molecule	Species	Description	Cat. No
PARP-3	Human	Human PARP3 cDNA Clone / ORF Clone	HG11190-M

PARP-3 Related Areas

Enzyme>>Other>>PARP-3

PARP-3 Alternative Names

PARP-3, PARP3, ADPRT3, ADPRTL2, ADPRTL3, IRT1, PADPRT-3 [Homo sapiens]

PARP-3, Parp3, A930002C11Rik, AW990611, Adprt3, Adprtl3, pADPRT-3 [Mus musculus]

PARP-3 Background

PARP-3 (poly (ADP-ribose) polymerase family, member 3) protein contains an N-terminal WGR (tryptophan-, glycine-, and arginine-rich) domain and a C-terminal catalytic domain. PARP-3 is a novel member of the PARP family of enzymes that synthesize poly(ADP-ribose) on themselves and other acceptor proteins. PARP-3 is highly expressed in the nuclei of epithelial cells forming the ducts of prostate, salivary glands, liver, and pancreas and in the neurons of terminal ganglia. The crystal structure of the human PARP-3 catalytic domain was determined recently, and was found to be highly similar to mammalian PARP-1 and PARP-2 catalytic domains. PARP-1 resides for part of the cell cycle in the centrosome and interacts with PARP-3. The presence of both PARP-1 and PARP-3 at the centrosome may link the DNA damage surveillance network to the mitotic fidelity checkpoint, and they are involved in DNA repair and genome maintenance.

PARP-3 Related Studies

1. Loseva O, et al. (2010) PARP-3 is a mono-ADP-ribosylase that activates PARP-1 in the absence of DNA. J Biol Chem. 285(11): 8054-60.
2. Lehtio L, et al. (2009) Structural basis for inhibitor specificity in human poly(ADP-ribose) polymerase-3. J Med Chem. 52(9): 3108-11.
3. Rouleau M, et al. (2009) Assessment of PARP-3 distribution in tissues of cynomolgous monkeys. J Histochem Cytochem. 57(7): 675-85.
4. Rouleau M, et al. (2007) PARP-3 associates with polycomb group bodies and with components of the DNA damage repair machinery. J Cell Biochem. 100(2): 385-401.
5. Augustin A, et al. (2003) PARP-3 localizes preferentially to the daughter centriole and interferes with the G1/S cell cycle progression. J Cell Sci. 116(Pt 8): 1551-62.