This product is an active protein and may elicit a biological response in vivo, handle with caution.
ADP ribosyltransferase (NAD+; poly (ADP ribose)
ADP ribosyltransferase diphtheria toxin like 3
NAD(+) ADP ribosyltransferase 3
NAD(+) ADP-ribosyltransferase 3
NAD+ ADP ribosyltransferase 3
Poly (ADP ribose) polymerase family, member 3
Poly (ADP ribose) synthetase 3
Poly [ADP-ribose] polymerase 3
Poly[ADP ribose] synthetase 3
Poly[ADP-ribose] synthase 3
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.
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.
According to PubMed:10329013, the N-terminal domain (54 amino acids) of isoform 2 is responsible for its centrosomal localization. The C-terminal region contains the catalytic domain.
Nucleus. Cytoplasm > cytoskeleton > centrosome. Cytoplasm > cytoskeleton > centrosome > centriole. Core component of the centrosome. Preferentially localized to the daughter centriole throughout the cell cycle. According to PubMed:16924674, 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.