PARP3 Antibody – Goat Polyclonal

Function: Involved in the base excision repair (BER) pathway, by catalyzing the poly(ADP-ribosyl)ation of a limited number of acceptor proteins involved in chromatin architecture and in DNA metabolism. This modification follows DNA damages and appears as an obligatory step in a detection/signaling pathway leading to the reparation of DNA strand breaks. May link the DNA damage surveillance network to the mitotic fidelity checkpoint. Negatively influences the G1/S cell cycle progression without interfering with centrosome duplication. Binds DNA. May be involved in the regulation of PRC2 and PRC3 complex-dependent gene silencing. Ref.7

Catalytic activity: NAD+ + (ADP-D-ribosyl)(n)-acceptor = nicotinamide + (ADP-D-ribosyl)(n+1)-acceptor.

Subunit structure: Interacts with PRKDC and PARP1. Interacts with XRCC5; the interaction is dependent on nucleic acids. Interacts with XRCC6; the interaction is dependent on nucleic acids. Interacts with EZH2, HDAC1, HDAC2, SUZ12, YY1, LRIG3 and LIG4. Ref.7

Subcellular location: Nucleus. Cytoplasm › cytoskeleton › microtubule organizing center › centrosome. Cytoplasm › cytoskeleton › microtubule organizing center › centrosome › centriole. Note: Core component of the centrosome. Preferentially localized to the daughter centriole throughout the cell cycle. According to Ref.7, it is almost exclusively localized in the nucleus and appears in numerous small foci and a small number of larger foci whereas a centrosomal location has not been detected. Ref.3 Ref.7

Tissue specificity: Widely expressed; the highest levels are in the kidney, skeletal muscle, liver, heart and spleen; also detected in pancreas, lung, placenta, brain, leukocytes, colon, small intestine, ovary, testis, prostate and thymus.

Domain: According to Ref.2, the N-terminal domain (54 amino acids) of isoform 2 is responsible for its centrosomal localization. The C-terminal region contains the catalytic domain.

Post-translational modification: Auto-poly(ADP)-ribosylation.

Sequence similarities: Contains 1 PARP alpha-helical domain.Contains 1 PARP catalytic domain.