PARP-3

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 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]

Summaries for PARP-3

Entrez Gene summary for PARP-3:

The protein encoded by this gene belongs to the PARP family. These enzymes modify nuclear proteins by poly-ADP-ribosylation, which is required for DNA repair, regulation of apoptosis, and maintenance of genomic stability. This gene encodes the poly(ADP-ribosyl)transferase 3, which is preferentially localized to the daughter centriole throughout the cell cycle. Alternatively spliced transcript variants encoding different isoforms have been identified

OMIM - description for PARP-3:

Activation of ADP-ribosyltransferases, such as ADPRTL3, is an early cellular response to DNA strand breaks. These enzymes modify nuclear proteins by poly-ADP-ribosylation, which is required for DNA repair, regulation of apoptosis, and maintenance of genomic stability.

Wikipedia summary for PARP-3:

Poly [ADP-ribose] polymerase 3 is an enzyme that in humans is encoded by the PARP3 gene. The protein encoded by this gene belongs to the PARP family. These enzymes modify nuclear proteins by poly-ADP-ribosylation, which is required for DNA repair, regulation of apoptosis, and maintenance of genomic stability. This gene encodes the poly(ADP-ribosyl)transferase 3, which is preferentially localized to the daughter centriole throughout the cell cycle. Alternatively spliced transcript variants encoding different isoforms have been identified

Human PARP-3 Protein General Information

 

• Protein names: Recommended name: Poly [ADP-ribose] polymerase 3 Short name=PARP-3
• Sequence length: 533 AA.
• 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.
• Sequence similarities: Contains 1 PARP alpha-helical domain. Contains 1 PARP catalytic domain.
• Post-translational modification: Auto-poly(ADP)-ribosylation.
• 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
• Subcellular location: Nucleus. Cytoplasm › cytoskeleton › centrosome. Cytoplasm › cytoskeleton › 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.
• 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.

General information above from UniProt

Function for PARP-3 Protein

UniProtKB:

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.

Genatlas:

• PARP-3 is involved in the base excision repair (BER) pathway, by catalysing the poly(ADP-ribosyl)ation of a limited number of acceptor proteins involved in chromatin architecture and in DNA metabolism
• PARP-3 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
• PARP-3 is involved in detection/signaling pathway leading to the reparation of DNA strand breaks
• nuclear protein involved in transcriptional silencing and in the cellular response to DNA damage
• molecular roles for PARP3 and APLF in chromosomal DNA double-strand break repair reactions (
• PARP-3 catalyzes the reaction of ADP ribosylation, a key posttranslational modification of proteins involved in different signaling pathways from DNA damage to energy metabolism and organismal memory

Homology for human PARP-3

• ortholog to murine Adprtl3
• homolog to ADPRT