poly [ADP-ribose] polymerase 3; PARP-3; hPARP-3; IRT1; NAD+ ADP-ribosyltransferase 3; ADPRT-3; poly[ADP-ribose] synthase 3; pADPRT-3 (PARP3 ADPRT3 ADPRTL3)
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Introduction
Also see poly[ADP-ribose]polymerase
Function
- role in the base excision repair pathway, by catalyzing poly-ADP-ribosylation of a limited number of acceptor proteins involved in chromatin architecture & in DNA metabolism
- poly-ADP-ribosylation follows DNA damage & appears as an obligatory step in a detection/signaling pathway leading to repair of DNA double-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 & PRC3 complex- dependent gene silencing
- auto-poly(ADP)-ribosylation
- interacts with PRKDC & PARP1
- interacts with XRCC5 (nucleic acid-dependent)
- interacts with XRCC6 (nucleic acid-dependent)
- interacts with EZH2, HDAC1, HDAC2, SUZ12, YY1, LRIG3 & LIG4
Structure
- the N-terminal domain (54amino acids) of isoform 2 may be responsible for its centrosomal localization
- the C-terminal region contains the catalytic domain
- contains 1 PARP alpha-helical domain
- contains 1 PARP catalytic domain
Compartment
- nucleus, cytoplasm, cytoskeleton, centrosome, centriole
- core component of the centrosome
- preferentially localized to the daughter centriole throughout the cell cycle
Alternative splicing
named isoforms=2
Expression
- widely expressed
- highest levels in the kidney, skeletal muscle, liver, heart & spleen
- also detected in pancreas, lung, placenta, brain, leukocytes, colon, small intestine, ovary, testis, prostate & thymus